Abstract
The shape and organization of the plasma membrane are influenced not only by the lipid bilayer and its integral membrane proteins, but also by structures lying either just inside or just outside of the cell that provide a scaffolding for the membrane. Structures that interact closely with the extracellular face of the membrane may act as an “exoskeleton.” Structures on the cytoplasmic face of the plasma membrane are generally considered to be part of the “cytoskeleton.” A subset of the cytoskeleton that associates primarily or exclusively with the plasma membrane has been termed the “membrane skeleton.” This chapter considers the biochemistry and morphology of the exoskeleton and of the membrane-associated cytoskeleton, how these two macromolecular complexes interact with the plasma membrane, and finally, how they interact with each other through receptors located in the plasma membrane. A major emphasis is placed on the role of these complexes in forming distinct membrane domains, enriched in particular integral membrane proteins with specific biological functions.
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References
Kirsch, J., Langosch, D., Prior, P., Littauer, U. Z., Schmitt, B., and Betz, H. (1991). The 93-kDa glycine receptor-associated protein binds to tubulin. J. Biol. Chem. 266:22242–22245.
Tilney, L. G., and Detmers, P. (1975). Actin in erythrocyte ghosts and its association with spectrin. J. Cell Biol. 66:508–520.
Tsukita, S., and Ishikawa, H. (1980). Cytoskeletal network underlying the human erythrocyte membrane. J. Cell Biol. 85:567–576.
Lange, Y., Hadesman, R. A., and Steck, T. L. (1982). Role of the reticulum in the stability and shape of the isolated human erythrocyte membrane. J. Cell Biol. 92:714–721.
Winograd, E., Hume, D., and Branton, D. (1991). Phasing the conformational unit of spectrin. Proc. Nat. Acad. Sci. USA 88: 10788–10791.
Yan, Y., Winograd, E., Viel, A., Cronin, T., Harrison, S. C., and Branton, D. (1993). Crystal structure of the repetitive segments of spectrin. Science 262:2027–2030.
Speicher, D. W., and Ursitti, J. A. (1994). Conformation of a mammoth protein. Curr. Biol. 4:154–157.
Lundberg, S., Lehto, V.-P, and Backman, L. (1992). Characterization of calcium binding to spectrins. Biochemistry 31:5665–5671.
Karinch, A. M., Zimmer, W. E., and Goodman, S. R. (1990). The identification and sequence of the actin-binding domain of human red blood cell ß-spectrin. J. Biol. Chem. 265:11833–11840.
Speicher, D. W., Weglarz, L., and DeSilva, T. M. (1992). Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. J. Biol. Chem. 267: 14775–14782.
Viel, A., and Branton, D. (1994). Interchain binding at the tail end of the Drosophila spectrin molecule. Proc. Natl. Acad. Sci. USA 91:10839–10843.
McGough, A. M., and Josephs, R. (1990). On the structure of erythrocyte spectrin in partially expanded membrane skeletons. Proc. Natl. Acad. Sci. USA 87:5208–5212.
Ursitti, J. A., and Wade, J. B. (1993). Ultrastructure and immuno-cytochemistry of the isolated human erythrocyte membrane skeleton. Cell Motil. Cytoskel. 25:30–42.
Shen, B. W., Josephs, R., and Steck, T. L. (1986). Ultrastructure of the intact skeleton of the human erythrocyte membrane. J. Cell Biol. 102:997–1006.
Liu, S.-C., Derick, L. H., and Palek, J. (1987). Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J. Cell Biol. 104:527–536.
Shotton, D. M., Burke, B. E., and Branton, D. (1979). The molecular structure of human erythrocyte spectrin: Biophysical and electron microscopic studies. J. Mol. Biol. 131:303–329.
Byers, T. J., and Branton, D. (1985). Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. USA 82:6153–6157.
Ursitti, J. A., Pumplin, D. W., Wade, J. B., and Bloch, R. J. (1991). Ultrastructure of the human erythrocyte cytoskeleton and its attachment to the membrane. Cell Motil. Cytoskel. 19:227–243.
Parry, D. A. D., Dixon, T. W., and Cohen, C. (1992). Analysis of the three-α-helix motif in the spectrin superfamily of proteins. Biophys. J. 61:858–867.
Bloch, R. J., and Pumplin, D. W. (1992). A model of spectrin as a concertina in the erythrocyte membrane skeleton. Trends Cell Biol. 2:186–189.
Kennedy, S. P., Weed, S. A., Forget, B. G., and Morrow, J. S. (1994). A partial structural repeat forms the heterodimer self-association site of all ß-spectrins. J. Biol. Chem. 269:11400–11408.
Elgsaeter, A., Stokke, B. T., Mikkelsen, A., and Branton, D. (1986). The molecular basis of erythrocyte shape. Science 234:1217–1223.
Ralston, G. B., and Dunbar, J. C. (1979). Salt and temperature-dependent conformation changes in spectrin from human erythrocyte membranes. Biochim. Biophys. Acta 579:20–30.
Morrow, J. S., Jr., Haigh, W. B., and Marchesi, V. T. (1981). Spectrin oligomers: A structural feature of the erythrocyte cytoskeleton. J. Supramol. Struct. Cell Biochem. 17:275–287.
Morrow, J. S., and Marchesi, V T. (1981). Self-assembly of spectrin oligomers in vitro: A basis for a dynamic cytoskeleton. J. Cell Biol. 88:463–468.
Liu, S.-C., Windisch, P., Kim, S., and Palek, J. (1984). Oligomeric states of spectrin in normal erythrocyte membranes: Biochemical and electron microscopic studies. Cell 37:587–594.
Vandekerckhove, J., and Weber, K. (1978). Mammalian cytoplasmic actins are the products of at least two genes and differ in primary structure in at least 25 identified positions from skeletal muscle actins. Proc. Natl. Acad. Sci. USA 75:1106–1110.
Vandekerckhove, J., and Weber, K. (1978). At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptide. J. Mol. Biol. 126:783–802.
Gunning, P., Ponte, P., Okayama, H., Engel, J., Blau, H., and Kedes, L. (1983). Isolation and characterization of full-length cDNA clones for human α-, ß- and T-actin mRNA’s: Skeletal but not cytoplasmic actins have an amino terminal cysteine that is subsequently removed. Mol. Cell Biol. 3:787–795.
Gimona, M., Vandekerckhove, J., Goethals, M., Herzog, M., Lando, Z., and Small, J. V (1994). ß-Actin specific monoclonal antibody. Cell Motil. Cytoskel. 27:108–116.
Pinder, J. C., and Gratzer, W. B. (1983). Structural and dynamic states of actin in the erythrocyte. J. Cell Biol. 96:768–775.
Siegel, D. L., and Branton, D. (1985). Partial purification and characterization of an actin-bundling protein, band 4.9, from human erythrocytes. J. Cell Biol. 100:775–785.
Fowler, V. M., Davis, J. Q., and Bennett, V (1985). Human erythrocyte myosin: Identification and purification. J. Cell Biol. 100:47–55.
Fowler, V. M., and Bennett, V. (1984). Erythrocyte membrane tropomyosin: Purification and properties. J. Biol. Chem. 259: 5978–5989.
Fowler, V. M. (1990). Tropomodulin. A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J. Cell Biol. 111:471–482.
Fowler, V. M., Sussman, M. A., Miller, P. G., Flucher, B. E., and Daniels, M. P. (1993). Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. J. Cell Biol. 120:411–420.
Fairbanks, G., Steck, T. L., and Wallach, D. F. H. (1971). Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2624.
Leto, T. L., and Marchesi, V. T. (1984). A structural model of human erythrocyte protein 4.1. J. Biol. Chem. 259:4603–4608.
Tyler, J. M., Reinhardt, B. N., and Branton, D. (1980). Associations of erythrocyte membrane proteins: Binding of purified bands 2.1 and 4.1 to spectrin. J. Biol. Chem. 255:7034–7039.
Cohen, C. M., and Langley, R. C., Jr. (1984). Functional characterization of human erythrocyte spectrin α and ß chains: Association with actin and erythrocyte protein 4.1. Biochemistry 23:4488–495.
Coleman, T. R., Harris, A. S., Mische, S. M., Mooseker, M. S., and Morrow, J. S. (1987). ß-Spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. J. Cell Biol. 104:519–526.
Correas, I., Leto, T. L., Speicher, D. W., and Marchesi, V. T. (1986). Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations. J. Biol. Chem. 261:3310–3315.
Correas, I., Speicher, D. W., and Marchesi, V. T. (1986). Structure of the spectrin-actin binding site of erythrocyte protein 4.1. J. Biol. Chem. 261:13362–13366.
Subrahmanyan, G., Bertics, R J., and Anderson, R. A. (1991). Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro. Proc. Natl. Acad. Sci. USA 88:5222–5226.
Fowler, V., and Taylor, D. L. (1980). Spectrin plus band 4.1 crosslink actin: Regulation by micromolar calcium. J. Cell Biol. 85: 361–376.
Tanaka, T., Kadowaki, K., Lazarides, E., and Sobue, K. (1991). Ca2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1. J. Biol. Chem. 266:1134–1140.
Anderson, J. P., and Morrow, J. S. (1987). The interaction of calmodulin with human erythrocyte spectrin: Inhibition of protein 4.1-stimulated actin binding. J. Biol. Chem. 262:6365–6372.
Mische, S. M., Mooseker, M. S., and Morrow, J. S. (1987). Erythrocyte adducin: A calmodulin-regulated actin-binding protein that stimulates spectrin-actin binding. J. Cell Biol. 105:2837–2845.
Gardner, K., and Bennett, V. (1986). A new erythrocyte membrane-associated protein with calmodulin binding activity: Identification and purification. J. Biol. Chem. 261:1339–1348.
Joshi, R., Gilligan, D. M., Otto, E., McLaughlin, T., and Bennett, V. (1991). Primary structure and domain organization of human a and ß adducin. J. Cell Biol. 115:665–675.
Cohen, C. M., and Foley, S. F. (1986). Phorbol ester- and Ca2+-dependent phosphorylation of human red cell membrane skeletal proteins. J. Biol. Chem. 261:7701–7709.
Hughes, C. A., and Bennett, V. (1995). Adducin: A physical model with implications for function in assembly of spectrin-actin complexes. J. Biol. Chem. 270:18990–18996.
Bennett, V. (1990). Spectrin-based membrane skeleton: A multipo-tential adaptor between plasma membrane and cytoplasm. Physiol. Rev. 70:1029–1065.
Gardner, K., and Bennett, V. (1987). Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328:359–362.
Cohen, C. M., and Foley, S. F (1984). Biochemical characterization of complex formation by human erythrocyte spectrin, protein 4.1 and actin. Biochemistry 23:6091–6098.
St-Onge, D., and Gicquaud, C. (1990). Research on the mechanism of interaction between actin and membrane lipids. Biochem. Bio-phys. Res. Commun. 167:40–47.
Williamson, P., Bateman, J., Kozarsky, K., Mattocks, K., Hermanowicz, N., Choe, H.-R., and Schlegel, R. A. (1982). Involvement of spectrin in the maintenance of phase-state asymmetry in the erythrocyte membrane. Cell 30:725–733.
Cohen, A. M., Liu, S.C., Derick, L. H., and Palek, J. (1986). Ultra-structural studies of the interaction of spectrin with phosphatidyl-serine liposomes. Blood 68:920–926.
Bennett, V., and Stenbuck, P. J. (1979). Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J. Biol. Chem. 254:2533–2541.
Bennett, V., and Stenbuck, P. J. (1979). The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature 280:468–473.
Bennett V. (1992). Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem. 267:8703–8706.
Platt, O. S., Lux, S. E., and Falcone, J. F. (1993). A highly conserved region of human erythrocyte ankyrin contains the capacity to bind spectrin. J. Biol. Chem. 268:24421–24426.
Hall, T. G., and Bennett, V. (1987). Regulatory domains of erythrocyte ankyrin. J. Biol. Chem. 262:10537–10545.
Davis, L. H., and Bennett, V. (1990). Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin. J. Biol. Chem. 265:10589–10596.
Gallagher, P. G., Tse, W. T., Scarpa, A. L., Lux, S. E., and Forget, B. G. (1992). Large number of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin. Trans. Assoc. Am. Physicians 105:268–277.
Kennedy, S. P., Warren, S. L., Forget, B. G., and Morrow, J. S. (1991). Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid ß-spectrin. J. Cell Biol. 115:267–277.
Bennett, V., and Stenbuck, P. J. (1980). Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane. J. Biol. Chem. 255:6424–6432.
Davis, L., Lux, S. E., and Bennett, V. (1989). Mapping the ankyrin-binding site of the human erythrocyte anion exchanger. J. Biol. Chem. 264:9655–9672.
Golan, D. E., and Veatch, W. (1980). Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photo-bleaching recovery: Evidence for control by cytoskeletal interactions. Proc. Natl. Acad. Sci. USA 77:2537–2541.
Tsuji, A., and Ohnishi, S.-I. (1986). Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state. Biochemistry 25: 6133–6139.
Anderson, R. A., and Lovrien, R. E. (1984). Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeleton. Nature 307:655–658.
Anderson, R. A., Correas, I., Mazzucco, C., Castle, J. D., and Marchesi, V. T. (1988). Tissue-specific analogues of erythrocyte protein 4.1 retain functional domains. J. Cell. Biochem. 37:269–284.
Pasternack, G. R., Anderson, R. A., Leto, T. L., and Marchesi, V. T. (1985). Interactions between protein 4.1 and band 3: An alternative binding site for an element of the membrane skeleton. J. Biol. Chem. 260:3676–3683.
Steiner, J. P., and Bennett, V. (1988). Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin. J. Biol. Chem. 263:14417–14425.
Lombardo, C. R., Weed, S. A., Kennedy, S. P., Forget, B. G., and Morrow, J. S. (1994). Beta II-spectrin (fodrin) and beta I sigma II spectrin (muscle) contain NH2- and COOH-terminal membrane association domains (MAD1 and MAD2). J. Biol. Chem. 269:29212–29219.
Davis, L. H., and Bennett, V. (1994). Identification of two regions of ßG spectrin that bind to distinct sites in brain membranes. J. Biol. Chem. 269:4409–4416.
Gallagher, P. G., and Forget, B. G. (1993). Spectrin genes in health and disease. Semin. Hematol. 30:4–21.
Lux, S. E., Tse, W. T., Menninger, J. C., John, K. M., Harris, P., Shalev, O., Chilcote, R. R., Marchesi, S. L., Watkins, P. C., Bennett, V., Mcintosh, S., Collins, F. S., Francke, U., Ward, D. C., and Forget, B. G. (1990). Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. Nature 345:736–739.
Conboy, J., Mohandas, N., Tchernia, G., and Kan, Y. W. (1986). Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency. N. Engl. J. Med. 315:680–685.
Winkelmann, J. C., and Forget, B. G. (1993). Erythroid and non-erythroid spectrins. Blood 81:3173–3185.
Levine, J., and Willard, M. (1981). Fodrin: Axonally transported polypeptides associated with the internal periphery of many cells. J. Cell Biol. 90:631–643.
Goodman, S. R., Zagon, I. S., and Kulikowski, R. R. (1981). Identification of a spectrin-like protein in nonerythroid cells. Proc. Natl. Acad. Sci. USA 78:7570–7574.
Davis, J., and Bennett, V. (1983). Brain spectrin. Isolation of sub-units and formation of hybrids with erythrocyte spectrin subunits. J. Biol. Chem. 258:7757–7766.
Wasenius, V.-M., Saraste, M., Salven, P., Eramaa, M., Holm, L., and Lehto, V.-P. (1989). Primary structure of the brain α-spectrin. J. Cell Biol. 108:79–93.
Harris, A. S., Croall, D. E., and Morrow, J. S. (1988). The calmodulin binding site in α-fodrin is near the calcium-dependent protease-I cleavage site. J. Biol. Chem. 263:15754–15761.
Merilainen, J., Palovuori, R., Sormunen, R., Wasneius, V.-M., and Lehto, V.-P. (1993). Binding of the α-fodrin SH3 domain to the leading lamellae of locomoting chicken fibroblasts. J. Cell Sci. 105:647–654.
Harris, A. S., Croall, D. E., and Morrow, J. S. (1989). Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease I. J. Biol. Chem. 264:17401–17408.
Harris, A. S., and Morrow, J. S. (1990). Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proc. Natl. Acad. Sci. USA 87:3009–3013.
Steiner, J. P., Walke, H. T., Jr., and Bennett, V (1989). Calcium/calmodulin inhibits direct binding of spectrin to synaptosomal membranes. J. Biol. Chem. 264:2783–2791.
Clark, M. B., Ma, Y., Bloom, M. L., Barker, J. E., Zagon, I. S., Zimmer, W. E., and Goodman, S. R. (1994). Brain erythroid a spectrin: Identification, compartmentalization and ß spectrin associations. Brain Res. 663:223–236.
Winkelmann, J. C., Costa, F. F., Linzie, B. L., and Forget, B. G. (1990). ß-Spectrin in human skeletal muscle—Tissue specific differential processing of a 3′ ß-spectrin pre-messenger RNA generates a ß-spectrin isoform with a unique carboxyl terminus. J. Biol. Chem. 265:20449–20454.
Porter, G. A., Dmytrenko, G. M., Winkelmann, J. C., and Bloch, R. J. (1991). Dystrophin colocalizes with ß-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J. Cell Biol. 117:997–1005.
Malchiodi-Albedi, F., Ceccarini, M., Winkelmann, J. C., Morrow, J. S., and Petrucci, T. C. (1993). The 270 kDa splice variant of erythrocyte ß-spectrin (ßIΣ2) segregates in vivo and in vitro to specific domains of cerebellar neurons. J. Cell Sci. 106:67–78.
Moon, R. T., and McMahon, A. P. (1990). Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human non-erythroid α-spectrin. J. Biol. Chem. 265:4427–4432.
Bloch, R. J., and Morrow, J. S. (1989). An unusual ß-spectrin associated with clustered acetylcholine receptors. J. Cell Biol. 108: 481–493.
Glenney, J., and Glenney, P. (1984). Co-expression of spectrin and fodrin in Friend erythroleukemic cells treated with DMSO. Exp. Cell Res. 152:15–21.
Riederer, B. M., Zagon, I. S., and Goodman, S. R. (1986). Brain spectrin (240/235) and brain spectrin (240/235E): Two distinct spectrin subtypes with different locations within mammalian neural cells. J. Cell Biol. 102:2088–2097.
Riederer, B. M., Lopresti, L. L., Krebs, K. E., Zagon, I. S., and Goodman, S. R. (1988). Brain spectrin (240/235) and brain spectrin (240/235E): Conservation of structure and location within mammalian neural tissue. Brain Res. Bull. 21:607–616.
Kunimoto, M., Otto, E., and Bennett, V (1991). A new 440-kD isoform is the major ankyrin in neonatal rat brain. J. Cell Biol. 115: 1319–1331.
Birkenmeier, C. S., White, R. A., Peters, L. L., Barker, J. E., and Lux, S. E. (1993). Complex patterns of sequence variation and multiple 5′ and 3′ ends are found among transcripts of the erythroid ankyrin gene. J. Biol. Chem. 268:9533–9540.
Otto, E., Kunimoto, M., McLaughlin, T., and Bennett, V. (1991). Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J. Cell Biol. 114:241–253.
Kordeli, E., Lambert, S., and Bennett, V. (1995). AnkyrinG: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J. Biol. Chem. 270:2352–2359.
Peters, L. L., John, K. M., Lu, F. M., Eicher, E. M., Higgins, A., Yialamas, M., Turtzo, L. C., Otsuka, A. J., and Lux, S. E. (1995). Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. J. Cell Biol. 130:313–330.
Ngai, J., Stack, J. H., Moon, R. T., and Lazarides, E. (1987). Regulated expression of multiple chicken erythroid membrane skeletal protein 4.1 variants is governed by differential RNA processing and translational control. Proc. Natl. Acad. Sci. USA 84:4432–4436.
Conboy, J. G., Chan, J., Mohandas, N., and Kan, Y. W. (1988). Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. Proc. Natl. Acad. Sci. USA 85:9062–9065.
Tang, T. K., Leto, T. L., Correas, I., Alonso, M. A., Marchesi, V. T., and Benz, E. J., Jr. (1988). Selective expression of an erythroid-specific isoform of protein 4.1. Proc. Natl. Acad. Sci. USA 85: 3713–3717.
Dhermy, D. (1991). The spectrin super-family. Biol. Cell 71:249–254.
Pumplin, D. W., and Bloch, R. J. (1993). The membrane skeleton. Trends Cell Biol. 3:113–117.
Ahn, A. H., and Kunkel, L. M. (1993). The structural and functional diversity of dystrophin. Nature Genet. 3:283–291.
Schofield, J. N., Blake, D. J., Simmons, C., Morris, G. E., Tinsley, J. M., Davies, K. E., and Edwards, Y. H. (1994). Apodystrophin-1 and apo-dystrophin-2, products of the Duchenne muscular dystrophy locus: Expression during mouse embryogenesis and in cultured cell lines. Hum. Mol. Genet. 3:1309–1316.
Lidov, H. G., Selig, S., and Kunkel, L. M. (1995). Dp140: A novel 140 kDa CNS transcript from the dystrophin locus. Hum. Mol. Genet. 4:329–335.
Koening, M., Monaco, A. P., and Kunkel, L. M. (1988). The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53:219–228.
Kahana, E., and Gratzer, W. B. (1995). Minimal folding unit of dystrophin rod domain. Biochemistry 34:8110–8114.
Hemmings, L., Kuhlman, P. A., and Critchely, D. R. (1992). Analysis of the actin-binding domain of α-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J. Cell Biol. 116:1369–1380.
Way, M., Pope, B., Cross, R. A., Kendrick-Jones, J., and Weeds, A. G. (1992). Expression of the N-terminal domain of dystrophin in E. coli and demonstration of binding to F-actin. FEBS Lett. 301:243–245.
Ervasti, J. M., and Campbell, K. P. (1993). A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122:809–823.
Campbell, K. P., and Kahl, S. D. (1989). Association of dystrophin and an integral membrane glycoprotein. Nature 338:259–262.
Yoshida, M., and Ozawa, E. (1990). Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem. 108:748–752.
Ervasti, J. M., and Campbell, K. P. (1991). Membrane organization of the dystrophin-glycoprotein complex. Cell 66:1121–1131.
Adams, M. E., Butler, M. H., Dwyer, T. M., Peters, M. F., Murnane, A. A., and Froehner, S. C. (1993). Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution. Neuron 11:531–540.
Kramarcy, N. R., Vidal, A., Froehner, S. C., and Sealock, R. (1994). Association of utrophin and multiple dystrophin short forms with the mammalian Mr 58,000 dystrophin-associated protein (syntrophin). J. Biol. Chem. 269:2870–2876.
Yang, B., Jung, D., Rafael, J. A., Chamerlain, J. S., and Campbell, K. P. (1995). Identification of α-syntrophin binding to syntrophin triplet, dystrophin and utrophin. J. Biol. Chem. 270:4975–4978.
Suzuki, A., Yoshida, M., and Ozawa, E. (1995). Mammalian aland ß1-syntrophin bind to the alternative splice-prone region of the dystrophin COOH terminus. J. Cell Biol. 128:373–381.
Ahn, A., and Kunkel, L. M. (1995). Syntrophin binds to an alternatively spliced exon of dystrophin. J. Cell Biol. 128:363–371.
Suzuki, A., Yoshida, M., Yamamoto, H., and Ozawa, E. (1992). Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain. FEBS Lett. 308:154–160.
Suzuki, A., Yoshida, M., Hayashi, K., Mizuno, Y., Hagiwara, Y., and Ozawa, E. (1994). Molecular organization at the glycoprotein-complex-binding site of dystrophin. Three dystrophin associated proteins bind directly to the carboxy-terminal portion of dystrophin. Eur. J. Biochem. 220:283–292.
Ibraghimov-Beskrovnaya, O., Ervasti, J. M., Leveille, C. J., Slaughter, C. A., Sernett, S. W., and Campbell, K. P. (1992). Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355:696–702.
Pons, F., Augier, N., Heilig, R., Leger, J., Mornet, D., and Leger, J. J. (1990). Isolated dystrophin molecules as seen by electron microscopy. Proc. Natl. Acad. Sci. USA 87:7851–7855.
Sato, O., Nonomura, Y., Kimura, S., and Maruyama, K. (1992). Molecular shape of dystrophin. J. Biochem. 112:631–636.
Dmytrenko, G. M., Pumplin, D. W., and Bloch, R. J. (1993). Membrane and cytoskeletal localization of dystrophin in cultured rat myotubes. J. Neurosci. 13:547–558.
Wakayama, Y (1991). Dystrophin is localized to the plasma membrane of human skeletal muscle fibers by electron-microscopic cytochemical study. Muscle Nerve 14:576–577.
Wakayama, Y., and Shibuya, S. (1991). Gold-labelled dystrophin molecule in muscle plasmalemma of mdx control mice as seen by electron microscopy of deep etching replica. Acta Neuropathol. 82:178–184.
Pardo, J. V., Siliciano, J. D., and Craig, S. W. (1983). A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements (“costameres”) mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. USA 80:1008–1012.
Pardo, J. V., Siliciano, J. D., and Craig, S. W. (1983). Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers. J. Cell Biol. 97:1081–1088.
Nelson, W. J., and Lazarides, E. (1984). Goblin (ankyrin) in striated muscle: Identification of the potential membrane receptor for erythroid spectrin in muscle cells. Proc. Natl. Acad. Sci. USA 81: 3292–3296.
Terrado, L., Gullberg, D., Rubin, K., Craig, S., and Borg, T. K. (1989). Expression of collagen adhesion proteins and their association with the cytoskeleton in cardiac myocytes. Anat. Rec. 223:62–71.
Lakonishok, M., Muschler, J., and Horwitz, A. F. (1992). The a5ßl integrin associates with a dystrophin-containing lattice during muscle development. Dev. Biol. 152:209–220.
Senter, L., Luise, M., Presotto, C., Betto, R., Teresi, A., Ceoldo, S., and Salviati, G. (1993). Interaction of dystrophin with cytoskeletal proteins: Binding to talin and actin. Biochem. Biophys. Res. Commun. 192:899–904.
Kramarcy, N. R, and Sealock, R. (1990). Dystrophin as a focal adhesion protein. Colocalization with talin and the Mr 48,000 sarcolemmal protein in cultured Xenopus muscle. FEBS Lett. 274:171–174.
Straub, V., Bittner, R. E., Leger, J. J., and Voit, T. (1992). Direct visualization of the dystrophin network on skeletal muscle fiber membrane. J. Cell Biol. 119:1183–1191.
North, A. J., Galazkiewicz, B., Byers, T. J., Glenney, J. R., Jr., and Small, J. V. (1993). Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle. J. Cell Biol. 120:1159–1167.
Khurana, T. S., Hoffman, E. P., and Kunkel, L. M. (1990). Identification of a chromosome 6-encoded dystrophin-related protein. J. Biol. Chem. 265:16717–16720.
Love, D. R., Hill, D. F., Dickson, G., Spurr, N. K., Byth, B. C., Marsden, R. F., Walsh, F. S., Edwards, Y H., and Davies, K. E. (1989). An autosomal transcript in skeletal muscle with homology to dystrophin. Nature 339:55–58.
Man, N. T., Thanh, L. T., Blake, D. J., Davies, K. E., and Morris, G. E. (1992). Utrophin, the autosomal homologue of dystrophin, is widely-expressed and membrane-associated in cultured cell lines. FEBS Lett. 313:19–22.
Man, N. T., Helliwell, T. R., Simmons, C., Winder, S. J., Kendrick-Jones, J., Davies, K. E., and Morris, G. E. (1995). Full-length and short forms of utrophin, the dystrophin-related protein. FEBS Lett. 358:262–266.
Winder, S. J., Hemmings, L., Maciver, S. K., Bolton, S. J., Simmons, C., Tinsley, J. M., Davies, K. E., Critchley, D. R., and Kendrick-Jones, J. (1995). Utrophin actin binding domain: Analysis of actin binding and cellular targeting. J. Cell Sci. 108:63–71.
Matsumura, K., Ervasti, J. M., Ohlendieck, K., Kahl, S. D., and Campbell, K. P (1992). Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature 360:588–591.
Ohlendieck, K., Ervasti, J. M., Matsumura, K., Kahl, S. D., Leveille, C. J., and Campbell, K. P. (1991). Dystrophin-related protein is localized to neuromuscular junctions of skeletal muscle. Neuron 7:499–508.
Campanelli, J. T., Roberds, S. L., Campbell, K. P., and Serieller, R. H. (1994). A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 77:663–674.
Phillips, W. D., Noakes, P. G., Roberds, S. L., Campbell, K. P., and Merlie, J. P. (1993). Clustering and immobilization of acetylcholine receptors by the 43-kD protein: A possible role for dystrophin-related protein. J. Cell Biol. 123:729–740.
Peters, M. F., Kramarcy, N. R., Sealock, R., and Froehner, S. C. (1944). ß2-Syntrophin: Localization at the neuromuscular junction in skeletal muscle. Neuroreport 5:1577–1580.
Pons, F., Augier, N., Leger, J. O. C., Robert, A., Tome, F. M. S., Fardeau, M., Voit, T., Nicholson, L. V. B., Mornet, D., and Leger, J. J. (1991). A homologue of dystrophin is expressed at the neuromuscular junctions of normal individuals and DMD patients, and of normal and mdx mice. FEBS Lett. 282:161–165.
Lidov, H. G. W., Byers, T. J., Watkins, S. C., and Kunkel, L. M. (1990). Localization of dystrophin to postsynaptic regions of central nervous system cortical neurons. Nature 348:725–728.
Khurana, T. S., Watkins, S. C., and Kunkel, L. M. (1992). The subcellular distribution of chromosome 6-encoded dystrophin-related protein in the brain. J. Cell Biol. 119:357–366.
Matsudaira, P. (1991). Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 17:87–92.
Davison, M. D., and Critchley, D. R. (1988). α-Actinins and the DMD protein contain spectrin-like repeats. Cell 52:159–160.
Davison, M.D., Baron, M. D., Critchley, D. R., and Wootton, J. C. (1989). Structural analysis of homologous repeated domains in α-actinin and spectrin. Int. J. Biol. Macromol. 11:81–90.
Gilmore, A. P., Parr, T., Patel, B., Gratzer, W. B., and Critchley, D. R. (1994). Analysis of the phasing of four spectrin-like repeats in α-actinin. Eur. J. Biochem. 225:235–242.
Otey, C. A., Pavalko, F. M., and Burridge, K. (1990). An interaction between α-actinin and the ß-1 integrin subunit in vitro. J. Cell Biol. 111:721–729.
Otey, C. A., Vasquez, G. B., Burridge, K., and Erickson, B. W. (1993). Mapping of the α-actinin binding site within the beta 1 integrin cytoplasmic domain. J. Biol. Chem. 268:21193–21197.
Lazarides, E., and Burridge, K. (1975). α-Actinin: Immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell 6:289–298.
Burridge, K., Fath, K., Kelly, T., Nuckolls, G., and Turner, C. (1988). Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487–525.
Street, S. F (1983). Lateral transmission of tension in frog myofibers: A myofibrillar network and transverse cytoskeletal connections are possible transmitters. J. Cell. Physiol. 114:346–364.
Pierobon-Bormioli, S. (1981). Transverse sarcomere filamentous systems: ‘Z- and M-cables.’ J. Muse. Res. Cell Modi. 2:401–413.
Garamvölgi, N. (1965). Inter-Z bridges in the flight muscle of the bee. J. Ultrastruct. Res. 13:435–443.
Shear, C. R., and Bloch, R. J. (1985). Vinculin in subsarcolemmal densities in chicken skeletal muscle: Localization and relationship to intracellular and extracellular structures. J. Cell Biol. 101:240–256.
Pasternak, C., Wong, S., and Elson, E. L. (1995). Mechanical function of dystrophin in muscle cells. J. Cell Biol. 128:355–361.
Hoffman, E. P., Fischbeck, K. H., Brown, R. H., Johnson, M., Medori, R., Loike, J. D., Harris, J. B., Waterston, R., Brooke, M., Specht, L., Kupsky, W., Chamberlain, J., Caskey, C. T., Shapiro, F., and Kunkel, L. M. (1988). Characterization of dystrophin in muscle-biopsy specimens from patients with Duchenne’s or Becker’s muscular dystrophy. N. Engl. J. Med. 318:1363–1368.
England, S. B., Nicholson, L. V. B., Johnson, M. A., Forrest, S. M., Love, D. R., Zubrzycka-Gaarn, E. E., Bulman, D. E., Harris, J. B., and Davies, K. E. (1990). Very mild muscular dystrophy associated with the deletion of 46% of dystrophin. Nature 343: 180–182.
Matsumura, K., Tome, F. M., Ionasescu, V., Ervasti, J. M., Anderson, R. D., Romero, N. B., Simon, D., Recan, D., Kaplan, J. C., Fardeau, M., et al. (1993). Deficiency of dystrophin-associated proteins in Duchenne muscular dystrophy patients lacking COOH-terminal domains of dystrophin. J. Clin. Invest. 92:866–871.
Matsumura, K., Burghes, A. H., Mora, M., Tome, F. M., Morandi, L., Cornello, F., Leturcq, F., Jeanpierre, M., Kaplan, J. C., Reinert, P., et al. (1994). Immunohistochemical analysis of dystrophin-associated proteins in Becker/Duchenne muscular dystrophy with huge in-frame deletions in the NH2-terminal and rod domains of dystrophin. J. Clin. Invest. 93:99–105.
Kobzik, L., Reid, M. B., Bredt, D. S., and Stamler, J. S. (1994). Nitric oxide in skeletal muscle. Nature 372:546–548.
Brenman, J. E., Chao, D. S., Zia, H. H., Aldape, K., and Bredt, D. S. (1995). Nitric oxide synthase complexed with dystrophin and absent from muscle sarcolemma in Duchenne muscular dystrophy. Cell 82:743–752.
Florence, J. M., Fox, P. T., Planer, G. J., and Brooke, M. H. (1985). Activity creatine kinase, and myoglobin in Duchenne muscular dystrophy: A clue to etiology? Neurology 35:758–761.
Webster, C., Silberstein, L., Hays, A. P., and Blau, H. M. (1988). Fast muscle fibers are preferentiailly affected in Duchenne’s muscular dystrophy. Cell 52:503–513.
Weiler, B., Karparti, G., and Carpenter, S. (1990). Dystrophin-deficient mdx muscle fibers are preferentially vulnerable to necrosis induced by experimental lengthening contractions. J. Neuro. Sci. 100:9–13.
Froehner, S. C., Murnane, A. A., Tobler, M., Peng H. B., and Sealock, R. (1987). A postsynaptic Mr 58,000 (58K) protein concentrated at acetylcholine receptor-rich sites in Torpedo electro-plaques and skeletal muscle. J. Cell Biol. 104:1633–1646.
Ohlendieck, K., and Campbell, K. P. (1991). Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J. Cell Biol. 115:1685–1694.
Ahn, A. H., Yoshida, M., Anderson, M. S., Feener, C. A., Selig, S., Hagiwara, Y., Ozawa, E., and Kunkel, L. M. (1994). Cloning of human basic Al, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8Q23–24. Proc. Natl. Acad. Sci. USA 91: 4446–4450.
Yang, B., Ibraghimov-Beskrovnaya, O., Moomaw, C. R., Slaughter, C. A., and Campbell, K. P. (1994). Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression. J. Biol. Chem. 269:6040–6044.
Matsumura, K., Tome, F. M. S., Collin, H., Azibi, K., Chaouch, M., Kaplan, J.-C., Fardeau, M., and Campbell, K. P. (1992). Deficiency of the 50K dystrophin-associated glycoprotein in severe childhood autosomal recessive muscular dystrophy. Nature 359:320–322.
Yamanouchi, Y., Mizuno, Y., Yamamoto, H., Takemitsu, M., Yoshida, M., Nonaka, U., and Ozawa, E. (1994). Selective defect in dystrophin-associated glycoproteins 50DAG (A2) and 35DAG (A4) in the dystrophic hamster: An animal model for severe childhood autosomal recessive muscular dystrophy (SCARMD). Neuromusc. Disorders 4:49–54.
Roberds, S. L., and Campbell, K. P. (1995). Adhalin mRNA and cDNA sequence are normal in the cardiomyopathic hamster. FEBS Lett. 364:245–249.
Campbell, K. P. (1995). Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage. Cell 80:675–679.
Nelson, W. J., Shore, E. S., Wang, A. Z., and Hammerton, R. W. (1990). Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells. J. Cell Biol. 110:349–357.
Nelson, W. J., and Hammerton, R. W. (1989). A membrane-cytoskeletal complex containing Na,K-ATPase, ankyrin and fodrin in Madin-Darby canine kidney (MDCK) cells: Implications for the biogenesis of epithelial cell polarity. J. Cell Biol. 108:893–902.
Nelson, W. J., and Veshnock, P. J. (1987). Ankyrin binding to (Na+ + K+) ATPase and implications for the organization of membrane domains in polarized cells. Nature 328:533–536.
Morrow, J. S., Cianci, C. D., Ardito, T., Mann, A. S., and Kashgarian, M. (1989). Ankyrin links fodrin to the a subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. J. Cell Biol. 108:455–465.
Davis, J., Davis, L., and Bennett, V. (1989). Diversity in membrane binding sites of ankyrins. Brain ankyrin, erythrocyte ankyrin, and processed erythrocyte ankyrin associate with distinct sites in kidney microsomes. J. Biol. Chem. 264:6417–6426.
Hu, R.-J., Moorthy, S., and Bennett, V. (1995). Expression of functional domains of betaG-spectrin disrupts epithelial morphology in cultured cells. J. Cell Biol. 128:1069–1080.
Gumbiner, B. (1987). Structure, biochemistry, and assembly of epithelial tight junctions. Am. J. Physiol. 253:C749–C758.
Srinivasan, Y., Elmer, L., Davis, J., Bennett, V., and Angelides, K. (1988). Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature 333:177–180.
Srinivasan, Y., Lewallen, M., and Angelides, K. J. (1992). Mapping the binding site on ankyrin for the voltage-dependent sodium channel from brain. J. Biol. Chem. 267:7483–7489.
Black, J. A., Friedman, B., Waxman, S. G., Elmer, L. W., and Angelides, K. J. (1989). Immuno-ultrastructural localization of sodium channels at nodes of Ranvier and perinodal astrocytes in rat optic nerve. Proc. Roy. Soc. London Ser. B 238:39–51.
Kordeli, E., and Bennett, V. (1991). Distinct ankyrin isoforms at neuron cell bodies and nodes of Ranvier resolved using ankyrin-deficient mice. J. Cell Biol. 1145:1243–1259.
Ichimura, T., and Ellisman, M. H. (1991). Three-dimensional fine structure of cytoskeletal-membrane interactions at nodes of Ranvier. J. Neurocytol. 20:667–681.
Davis, J. Q., and Bennett, V. (1984). Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel. J. Biol. Chem. 259:13550–13559.
Langley, R. C., Jr., and Cohen, C. M. (1986). Association of spectrin with desmin intermediate filaments. J. Cell Biochem. 30:101–109.
Davis, J. Q., McLaughlin, T., and Bennett, V. (1993). Ankyrin-binding proteins related to nervous system cell adhesion molecules: Candidates to provide transmembrane and intercellular connections in adult brain. J. Cell Biol. 121:121–133.
Peters, L. L., Birkenmeier, C. S., Bronson, R. T., White, R. A., Lux, S. E., Otto, E., Bennett, V., Higgins, A., and Barker, J. E. (1991). Purkinje cell degeneration associated with erythroid ankyrin deficiency in nb/nb mice. J. Cell Biol. 114:1233–1241.
Bloch, R. J., and Geiger, B. (1980). The localization of acetylcholine receptor clusters in areas of cell-substrate contact in cultures of rat myotubes. Cell 21:25–35.
Pollerberg, G. E., Burridge, K., Krebs, K. E., Goodman, S. R., and Schachner, M. (1987). The 180-kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions. Cell Tissue Res. 250:227–236.
Lombardo, C. R., Rimm, D. L., Kennedy, S. P., Forget, B. G., and Morrow, J. S. (1993). Ankyrin independent membrane sites for non-erythroid spectrin. Mol. Biol. Cell 4:57.
Otto, J. J. (1990). Vinculin. Cell Motil. Cytoskel. 16:1–6.
Geiger, B. (1979). A 130K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18:193–205.
Feramisco, J. R., and Burridge, K. (1980). A rapid purification of α-actinin, filamin, and a 130,000-dalton protein from smooth muscle J. Biol. Chem. 255:1194–1199.
Wachsstock, D. H., Wilkins, J. A., and Lin, S. (1987). Specific interaction of vinculin with α-actinin. Biochem. Biophys. Res. Commun. 146:554–560.
Geiger, B. (1982) Microheterogeneity of avian and mammalian vinculin distinctive subcellular distribution of different isovinculins. J. Mol. Biol. 159:685–701.
Price, G. J., Jones, P., Davison, M. D., Patel, B., Bendori, R., Geiger, B., and Critchley, D. R. (1989). Primary sequence and domain structure of chicken vinculin. Biochem. J. 259:453–461.
Bendori, R., Salomon, D., and Geiger, B. (1989). Identification of two distinct functional domains on vinculin involved in its association with focal contacts. J. Cell Biol. 108:2383–2393.
Molony, L., and Burridge, K. (1985). Molecular shape and self-association of vinculin and meta-vinculin. J. Cell Biochem. 29: 31–36.
Turner, C. E., Glenney, J. R., and Burridge, K. (1990). Paxillin—a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111:1059–1068.
Koteliansky, V. E., Ogryzko, E. P., Zhidkova, N. I., Weiler, P. A., Critchley, D. R., Vancompernolle, K., Vandekerckhove, J., Strasser, P., Way, M., Gimona, M., and Small, J. V. (1992). An additional exon in the human vinculin gene specifically encodes meta-vinculin-specific difference peptide. Cross-species comparison reveals variable and conserved motifs in the meta-vinculin insert. Eur. J. Biochem. 204:767–772.
Feramisco, J. R., Smart, J. E., Burridge, K., Helfman, D. M., and Thomas, G. P. (1982). Co-existence of vinculin and a vinculin-like protein of higher molecular weight in smooth muscle. J. Biol. Chem. 257:11024–11031.
Glukhova, M. A., Kabakov, A. E., Belkin, A. M., Frid, M. G., Ornatsky, O. I., Zhidkova, N. I., and Koteliansky, V. E. (1986). Metavinculin distribution in adult human tissues and cultured cells. FEBS Lett. 207:139–141.
Gilmore, A. P., Jackson, P., Waites, G. T., and Critchley, D. R. (1992). Further characterisation of the talin-binding site in the cytoskeletal protein vinculin. J. Cell Sci. 103:719–731.
Beckerle, M. C., and Yeh, R. K. (1990). Talin: Role at sites of cell-substratum adhesion. Cell Motil. Cytoskel. 16:7–13.
Molony, L., McCaslin, D., Abernethy, J., Paschal, B., and Burridge, K. (1987). Properties of talin from chicken gizzard smooth muscle. J. Biol. Chem. 282:7790–7795.
Burridge, K., and Mangeat, P. (1984). An interaction between vinculin and talin. Nature 308:744–746.
Burridge, K., Turner, C. E., and Romer, L. H. (1992). Tyrosine phosphorylation of paxillin and ppl25FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly. J. Cell Biol. 119:893–903.
Lo, S. H., Janmey, P. A., Hartwig, J. H., and Chen, L. B. (1994). Interactions of tensin with actin and identification of its three distinct actin-binding domains. J. Cell Biol. 125:1067–1075.
Chuang, J. Z., Lin, D. C., and Lin, S. (1995). Molecular cloning, expression, and mapping of the high affinity, actin-capping domain of chicken cardiac muscle. J. Cell Biol. 128:1095–1109.
Davis, S., Lu, M. L., Lo, S. H., Lin, S., Butler, J. A., Druker, B. J., Roberts, T. M., An, Q., and Chen, L. B. (1991). Presence of an SH2 domain in the actin-binding protein tensin. Science 252:712–715.
Horwitz, A. F., Duggan, K., Buck, C., Beckerle, M. C., and Burridge, K. (1986). Interaction of plasma membrane fibronectin with talin—A transmembrane linkage. Nature 320:531–533.
Rohrschneider, L. R. (1980). Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc. Natl. Acad. Sci. USA 77:3514–3518.
Hirst, R., Horwitz, A., Buck, C., and Rohrschneider, L. (1986). Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases. Proc. Natl. Acad. Sci USA 83:6470–6474.
Kornberg, L., Earp, H. S., Parsons, J. T., Schaller, M., and Juliano, R. L. (1992). Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267:23439–23442.
Samuelsson, S. J., Luther, P. W., Pumplin, D. W., and Bloch, R. J. (1993). Structures linking microfilament bundles to the membrane at focal contacts. J. Cell Biol. 122:485–496.
Pavalko, F. M., Schneider, G., Burridge, K., and Lim, S. S. (1995). Immunodetection of α-actinin in focal adhesions is limited by antibody inaccessibility. Exp. Cell Res. 217:534–540.
Yurchenco, P. D. (1990). Assembly of basement membranes. Ann. N.Y. Acad. Sci. 580:195–213.
Engel, J. (1992). Laminins and other strange proteins. Biochemistry 31:10643–10651.
Timpl, R., and Brown, J. C. (1994). The laminins. Matrix Biol. 14:275–281.
Burgeson, R. E., Chiquet, M., Deutzmann, R., Ekblom, P., Engel, J., Kleinman, H., Martin, G. R., Meneguzzi, G., Paulsson, M., Sanes, J., et al. (1994). A new nomenclature for the laminins. Matrix Biol. 14:209–211.
Mecham, R. P. (1991). Receptors for laminin on mammalian cells. FASEB J. 5:2538–2546.
Yurchenco, P. D., Sung, U., Ward, M. D., Yamada, Y., and O’Rear, J. J. (1993). Recombinant laminin G domain mediates myoblast adhesion and heparin binding. J. Biol. Chem. 268:8356–8365.
Mayer, U., Nischt, R., Poschl, E., Mann, K., Fukuda, K., Gerl, M., Yamada, Y., and Timpl, R. (1993). A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 12:1879–1885.
Gerl, M., Mann, K., Aumailley, M., and Timpl, R. (1991). Localization of a major nidogen-binding site to domain III of laminin B2 chain. Eur. J. Biochem. 202:167–174.
Colognato-Pyke, H., O’Rear, J. J., Yamada, Y., Carbonetto, S., Cheng, Y. S., and Yurchenco, P. D. (1995). Mapping of network-forming, heparin-binding, and α1ß1 integrin-recognition sites within the α-chain short arm of laminin-1. J. Biol. Chem. 270: 9398–9406.
Lievo, I., and Engvall, E. (1988). A protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development. Proc. Natl. Acad. Sci. USA 85:1544–1548.
Hunter, D. D., Shah, V., Merlie, J. P., and Sanes, J. R. (1989). A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature 338:229–234.
Gerecke, D. R., Wagman, D. W., Champliaud, M.-R., and Burgeson, R. E. (1994). The complete primary structure for a novel laminin chain, the laminin Blk chain. J. Biol. Chem. 269:11073–11080.
Vailly, J., Verrando, P., Champliaud, M. F., Gerecke, D., Wagman, D. W., Baudoin, C., Aberdam, D., Burgeson, R., Bauer, E., and Ortonne, J.-P. (1994). The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant. Eur. J. Biochem. 219:209–218.
Utani, A., Nomizu, M., Timpl, R., Roller, P. P., and Yamada, Y (1994). Laminin chain assembly. Specific sequences at the C terminus of the long arm are required for the formation of specific double- and triple-stranded coiled-coil structures. J. Biol. Chem. 269:19167–19175.
Kammerer, R. A., Antonsson, P., Schulthess, T., Fauser, C., and Engel, J. (1995). Selective chain recognition in the C-terminal α-helical coiled-coil region of laminin. J. Mol. Biol. 250:64–73.
Yurchenco, P. D., Cheng, Y.-S., and Schittny, J. C. (1990). Heparin modulation of laminin polymerization. J. Biol. Chem. 265:3981–3991.
Yurchenco, P. D., Cheng, Y.-S., and Colognato, H. (1992). Laminin forms an independent network in basement membranes. J. Cell Biol. 117:1119–1133.
Schittny, J. C., and Yurchenco, P. D. (1990). Terminal short arm domains of basement membrane laminin are critical for its self-assembly. J. Cell Biol. 110:825–832.
Leivo, I., Vaheri, A., Timpl, R., and Wartiovaara, J. (1980). Appearance and distribution of collagens and laminin in the early mouse embryo. Dev. Biol. 76:100–114.
Fox, J. W., Mayer, U., Nischt, R., Aumailley, M., Reinhardt, D., Wiedemann, H., Mann, K., Timpl, R., Krieg, T., Engel, J., and Chu, M.-L. (1991). Recombinant nidogen consists of three globular domains and mediates binding of laminin to collagen type IV. EMBO J. 10:3137–3146.
Nagayoshi, T., Sanborn, D., Hickok, N. J., Olsen, D. R., Fazio, M. J., Chu, M.-L., Knowlton, R., Mann, K., Deutzmann, R., Timpl, R., and Uitto, J. (1989). Human nidogen: Complete amino acid sequence and structural domains deduced from cDNAs, and evidence for polymorphism of the gene. DNA 8:581–594.
Reinhardt, D., Mann, K., Nischt, R., Fox, J. W., Chu, M.-L., Krieg, T., and Timpl, R. (1993). Mapping of nidogen binding sites for collagen type IV, heparan sulfate proteoglycan, and zinc. J. Biol. Chem. 268:10881–10887.
Noonan, D. M., Fülle, A., Valente, P., Cai, S., Horigan, E., Sasaki, M., Yamada, Y., and Hassell, J. R. (1991). The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule. J. Biol. Chem. 266:22939–22947.
Laurie, G. W., Inoue, S., Bing, J. T., and Hassell, J. R. (1988). Visualization of the large heparan sulfate proteoglycan from basement membrane. Am. J. Anat. 181:320–326.
Yurchenco, P. D., Cheng, Y.-S., and Ruben, G. C. (1987). Self-assembly of high molecular weight basement membrane heparan sulfate proteoglycan into dimers and oligomers. J. Biol. Chem. 262:17668–17676.
Battaglia, C., Mayer, U., Aumailley, M., and Timpl, R. (1992). Basement-membrane heparan sulfate proteoglycan binds to laminin by its heparan sulfate chains and to nidogen by sites in the protein core. Eur. J. Biochem. 208:359–366.
Ali, I. U., Mautner, V., Lanza, R., and Hynes, R. O. (1977). Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell 11:115–126.
Yamada, K. M., and Weston, J. A. (1974). Isolation of a major cell surface glycoprotein from fibroblasts. Proc. Natl. Acad. Sci. USA 71:3492–3496.
Yamada, K. M., Yamada, S. S., and Pastan, I. (1976). Cell surface protein partially restores morphology, adhesiveness, and contact inhibition of movement to transformed fibroblasts. Proc. Natl. Acad. Sci. USA 73:1217–1221.
Hynes, R. O., and Yamada, K. M. (1982). Fibronectins: Multifunctional modular glycoproteins. J. Cell Biol. 95:369–377.
Hynes, R. O. (1990). Fibronectins, Springer-Verlag, Berlin.
Hynes, R. O. (1993). Fibronectins. In Guidebook to the Extracellular Matrix and Adhesion Proteins (T. Kreis and R. Vale, eds.), Oxford University Press, London, pp. 56–58.
Paul, J. I., Schwarzbauer, J. E., Tamkun, J. W., and Hynes, R. O. (1986). Cell-type-specific fibronectin subunits generated by alternative splicing. J. Biol. Chem. 261:12258–12265.
Colombi, M., Barlati, S., Kornblihtt, A., Baralle, F. E., and Vaheri, A. (1986). A family of fibronectin mRNAs in human normal and transformed cells. Biochim. Biophys. Acta 868:207–214.
Hayashi, M., and Yamada, K. M. (1981). Differences in domain structures between plasma and cellular fibronectins. J. Biol. Chem. 256:11292–11300.
Tamkun, J. W., Schwarzbauer, J. E., and Hynes, R. O. (1984). A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon. Proc. Natl. Acad. Sci. USA 81:5140–5144.
Hirano, H., Yamada, Y., Sullivan, M., DeCroimbrugghe, B., Pastan, I., and Yamada, K. M. (1983). Isolation of genomic DNA clones spanning the entire fibronectin gene. Proc. Natl. Acad. Sci. USA 80:46–50.
Ruoslahti, E., Hayman, E. G., Kuusela, P., Shively, J. E., and Engvall, E. (1979). Isolation of a tryptic fragment containing the collagen-binding site of plasma fibronectin. J. Biol. Chem. 254:6054–6059.
Hayashi, M., Schlesinger, D. H., Kennedy, D. W., and Yamada, K. M. (1980). Isolation and characterization of a heparin-binding domain of cellular fibronectin. J. Biol. Chem. 255:10017–10020.
Wagner, D. D., and Hynes, R. O. (1980). Topological arrangement of the major structural features of fibronectin. J. Biol. Chem. 255: 4304–4312.
Ruoslahti, E., Hayman, E. G., and Engvall, E. (1981). Alignment of biologically active domains in the fibronectin molecule. J. Biol. Chem. 256:7277–7281.
Dickinson, C. D., Gay, D. A., Parello, J., Ruoslahti, E., and Ely, K. R. (1994). Crystals of the cell-binding module of fibronectin obtained from a series of recombinant fragments differing in length. J. Mol. Biol. 238:123–127.
Dickinson, C. D., Veerapandian, B., Dai, X. P., Hamlin, R. C., Xuong, N. H., Ruoslahti, E., and Ely, K. R. (1994). Crystal structure of the tenth type III cell adhesion module of human fibronectin. J. Mol. Biol. 236:1079–1092.
Wu, C., Bauer, J. S., Juliano, R. L., and McDonald, J. A. (1993). The a5ßl integrin fibronectin receptor, but not the α5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J. Biol. Chem. 268:21883–21888.
Singer, I. I. (1979). The fibronexus: A transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts. Cell 16:675–685.
Ruoslahti, E., and Pierschbacher, M. D. (1987). New perspectives in cell adhesion: RGD and integrins. Science 238:491–497.
Hynes, R. O. (1987). Integrins: A family of cell surface receptors. Cell 48:549–554.
Hynes, R. O. (1992). Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11–25.
Albelda, S. M., and Buck, C. A. (1990). Integrins and other cell adhesion molecules. FASEB J. 4:2868–2880.
Ruoslahti, E. (1988). Fibronectin and its receptor. Annu. Rev. Biochem. 57:375–413.
Pierschbacher, M., Hayman, E. G., and Ruoslahti, E. (1983). Synthetic peptide with cell attachment activity of fibronectin. Proc. Natl. Acad. Sci. USA 80:1224–1227.
Pytela, R., Pierschbacher, M. D., and Ruoslahti, E. (1985). Identification and isolation of a 140 kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 40:191–198.
Suzuki, S., Argraves, W. S., Pytela, R., Arai, H., Krusius, T., Pierschbacher, M. D., and Ruoslahti, E. (1986). cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors. Proc. Natl. Acad. Sci. USA 83:8614–8618.
Pytela, R., Pierschbacher, M. D., and Ruoslahti, E. (1985). A 125/115-kDa cell surface receptor specific for vitronectin interacts with the arginine-glycine-aspartic acid adhesion sequence derived from fibronectin. Proc. Nad. Acad. Sci. USA 82:5766–5770.
Neff, N. T., Lowrey, C., Decker, C., Tovar, A., Damsky, C., Buck, C., and Horwitz, A. F. (1982). A monoclonal antibody detaches embryonic skeletal muscle from extracellular matrices. J. Cell Biol. 95:654–666.
Horwitz, A. F., Duggan, K., Greggs, R., Decker, C., and Buck, C. (1985). The cell substrate attachment (CSAT) antigen has properties of a receptor for laminin and fibronectin. J. Cell Biol. 101: 2134–2144.
Damsky, C. H., Knudsen, K. A., Bradley, D., Buck, C. A., and Horwitz, A. F. (1985). Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture. J. Cell Biol. 100:1528–1539.
Nermut, M. V., Green, N. M., Eason, P., Yamada, S. S., and Yamada, K. M. (1988). Electron microscopy and structural model of human fibronectin receptor. EMBO J. 7:4093–4099.
Kirchhofer, D., Gailit, J., Ruoslahti, E., Grzesiak, J., and Pierschbacher, M. D. (1990). Cation-dependent changes in the binding specificity of the platelet receptor GPIIIb/IIIa. J. Biol. Chem. 265: 18525–18530.
Smith, J. W., and Cheresh, D. A. (1990). Integrin (αvß3)-ligand interaction: Identification of a heterodimeric RGD binding site on the vitronectin receptor. J. Biol. Chem. 265:2168–2172.
D’Souza, S. E., Ginsberg, M. H., Burke, T. A., and Plow, E. F (1990). The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its a subunit. J. Biol. Chem. 265:3440–3446.
Loftus, J. C., O’Toole, T. E., Plow, E. F., Glass, A., Frelinger, A. L., III, and Ginsberg, M. H. (1990). A ß3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 249:915–918.
Pierschbacher, M. D., and Ruoslahti, E. (1987). Influence of stereochemistry of the sequence of Arg-Gly-Asp-Xaa on binding specificity in cell adhesion. J. Biol. Chem. 262:17294–17298.
Mould, A. P., Wheldon, L. A., Komoriya, A., Wayner, E. A., Yamada, K. M., and Humphries, M. J. (1990). Affinity chromatographic isolation of the melanoma adhesion receptor for the IIICS region of fibronectin and its identification as the integrin a4ß1. J. Biol. Chem. 265:4020–4024.
Gehlsen, K. R., Dillner, L., Engvall, E., and Ruoslahti, E. (1988). The human laminin receptor is a member of the integrin family of cell adhesion receptors. Science 241:1228–1229.
Kirchhofer, D., Languino, L. R., Ruoslahti, E., and Pierschbacher, M. D. (1990). α2ß1 integrins from different cell types show different binding specificities. J. Biol. Chem. 265:615–618.
Cheresh, D. A., and Klier, F. G. (1986). Asialoganglioside GD2 distributes preferentially into substrate-associated microprocesses on human melanoma cells during their attachment to fibronectin. J. Cell Biol. 102:1887–1897.
Yamada, K. M., Critchley, D. R., Fishman, P. H., and Moss, J. (1983). Exogenous gangliosides enhance the interaction of fibronectin with ganglioside-deficient cells. Exp. Cell Res. 143: 295–302.
Brown, E., Hooper, L., Ho, T., and Gresham, H. (1990). Integrin-associated protein: A 50 kDa plasma membrane antigen physically and functionally associated with integrin. J. Cell Biol. 111: 2785–2794.
Agraves, W. S., Dickerson, K., Burgess, W. H., and Ruoslahti, E. (1990). Fibulin, a novel protein that interacts with the fibronectin receptor ß subunit cytoplasmic domain. Cell 58:623–629.
Regen, C. M., and Horwitz, A. F. (1992). Dynamics of ß1 integrin-mediated adhesive contacts in motile fibroblasts. J. Cell Biol. 119: 1347–1359.
Singer, I.I., Scott, S., Kawka, D. W., Kazazis, D. M., Gailit, J., and Ruoslahti, E. (1988). Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation. J. Cell Biol. 106:2171–2182.
LaFlamme, S. E., Akiyama, S. K., and Yamada, K. M. (1992). Regulation of fibronectin receptor distribution. J. Cell Biol. 117: 437–447.
Wayner, E. A., Orlando, R. A., and Cheresh, D. A. (1991). Integrins avß3 and avß5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface. J. Cell Biol. 113:919–929.
Fath, K. R., Edgell, C.-J. S., and Burridge, K. (1989). The distribution of distinct integrins in focal contacts is determined by the substratum composition. J. Cell Sci. 92:67–75.
Juliano, R. L., and Haskill, S. (1993). Signal transduction from the extracellular matrix. J. Cell Biol. 120:577–585.
Chen, W.-T., Greve, J. M., Gottlieb, D. I., and Singer, S. J. (1985). Immunocytochemical localization of 140 kD cell adhesion molecules in cultured chicken fibroblasts, and in chicken smooth muscle and intestinal epithelial tissues. J. Histochem. Cytochem. 33:576–586.
Schaller, M. D., Parsons, J. T. (1994). Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 6:705–710.
Schaller, M. D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J.T. (1992). pp125FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA 89:5192–5196.
Lipfert, L., Haimovich, B., Schaller, M. D., Cobb, B. S., Parsons, J. T., and Brugge, J. S. (1992). Integrin-dependent phosphorylation and activation of the protein tyrosine kinase ppl25FAK in platelets. J. Cell Biol. 119:905–912.
Reynolds, A. B., Rosel, D. J., Kanner, S. B., and Parsons, J. T. (1989). Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene. Mol. Cell. Biol. 9:629–638.
Nigg, E. A., Sefton, B. M., Hunter, T., Walter, G., and Singer, S. J. (1982). Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc. Natl. Acad. Sci. USA 79:5322–5326.
Huhtala, P., Humphries, M. J., McCarthy, J. B., Tremble, P. M., Werb, Z., and Damsky, C. H. (1995). Cooperative signaling by α5ß1 and α4ß1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J. Cell Biol. 129:867–879.
Tremble, P. M., Damsky, C. H., and Werb, Z. (1995). Components of nuclear signaling cascade that regulate collagenase gene expression in response to integrin-derived signals. J. Cell Biol. 129: 1707–1720.
Ginsberg, M. H., Du, X., and Plow, E. F. (1992). Inside-out integrin signalling. Curr. Opin. Cell Biol. 4:766–771.
Sims, P. J., Ginsberg, M. H., Plow, E. F., and Shattil, S. J. (1991). Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 266:7345–7352.
Chen, Y.-P, O’Toole, T. E., Shipley, T., Forsyth, J., LaFlamme, S. E., Yamada, K. M., Shattil, S. J., and Ginsberg, M. H. (1994). “Inside-out” signal transduction inhibited by isolated integrin cytoplasmic domains. J. Biol. Chem. 269:18307–18310.
Vlodavsky, I., Bar-Shavit, R., Ishai-Michaeli, R., Bashkin, P., and Fuks, Z. (1991). Extracellular sequestration and release of fibroblast growth factor: A regulatory mechanism? Trends Biochem. Sci. 16:268–271.
Gitay-Cohen, H., Soker, S., Vlodavsky, I., and Neufeld, G. (1992). The binding of vascular endothelial growth factor to its receptors is dependent on cell surface-associated heparin-like molecules. J. Biol. Chem. 267:6093–6098.
Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991). Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64:841–848.
Kokenyesi, R., and Bernfield, M., (1994). Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1. J. Biol. Chem. 269:12304–12309.
Ohlendieck, K., Ervasti, J. M., Snook, J. B., and Campbell, K. P. (1991). Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol. 112:135–148.
Brancaccio, A., Schulthess, T., Gesemann, M., and Engel, J. (1995). Electron microscopic evidence for a mucin-like region in chick muscle α-dystroglycan. FEBS Lett. 368:139–142.
Hagiwara, Y., Yoshida, M., Nonaka, I., and Ozawa, E. (1989). Developmental expression of dystrophin on the plasma membrane of rat muscle cells. Protoplasma 151:11–18.
Tome, F. M., Evangelista, T., Leclerc, A., Sunada, Y., Manole, E., Estournet, B., Barois, A., Campbell, K. P., and Fardeau, M. (1994). Congenital muscular dystrophy with merosin deficiency. C. R. Acad. Sci. Ser. C 317:351–357.
Xu, H., Christmas, P., Wu, X.-R., Wewer, U. M., and Engvall, E. (1994). Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse. Proc. Natl. Acad. Sci. USA 91:5572–5576.
Ushkaryov, Y. A., Petrenko, A. G., Geppert, M., and Sudhof, T. C., (1992). Neurexins: Synaptic cell surface proteins related to the α-latrotoxin receptor and laminin. Science 257:50–56.
Sugrue, S. P., and Hay, E. D. (1981). Response of basal epithelial cell surface and cytoskeleton to solubilized extracellular matrix molecules. J. Cell Biol. 91:45–54.
Sanes, J. R., Engvall, E., Butkowski, R., and Hunter, D. D. (1990). Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. J. Cell Biol. 111:1685–1699.
McMahan, U. J., Sanes, J. R., and Marshall, L. M. (1978). Acetylcholinesterase is associated with the basal lamina at the neuromuscular junction. Nature 193:281–282.
Brandan, E., Maldonado, M., Garrido, J., and Inestrosa, N. C. (1985). Anchorage of collagen-tailed acetylcholinesterase to the extracellular matrix is mediated by heparan sulfate proteoglycans. J. Cell Biol. 101:985–992.
Fertuck, H. C., and Salpeter, M. M. (1976). Quantitation of junctional and extrajunctional acetylcholine receptors by electron microscope autoradiography after 125I-α-bungarotoxin binding at mouse neuromuscular junctions. J. Cell Biol. 69:144–158.
Heuser, J. E., and Salpeter, S. R. (1979). Organization of acetylcholine receptors in quick-frozen, deep-etched, and rotary-replicated Torpedo postsynaptic membrane. J. Cell Biol. 82:150–173.
Froehner, S. C. (1991). The sub-membrane machinery for nicotinic acetylcholine receptor clustering. J. Cell Biol. 114:1–7.
Marshall, L. M., Sanes, J. R., and McMahan, U. J. (1977). Reinnervation of original synaptic sites on muscle fiber basement membrane after disruption of the muscle cells. Proc. Natl. Acad. Sci. USA 74:3073–3077.
Hunter, D. D., Cashman, N., Morris-Valero, R., Bulock, J. W., Adams, S. P., and Sanes, J. R. (1991). An LRE (leucine-arginine-glutamate)-dependent mechanism for adhesion of neurons to Slaminin. J. Neurosci. 11:3960–3971.
Porter, B. E., Weis, J., and Sanes, J. R. (1995). A motoneuron-selective stop signal in the synaptic protein S-laminin. Neuron 14: 549–559.
Noakes, P. G., Gautam, M., Mudd, J., Sanes, J. R., and Merlie, J. P. (1995). Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin ß2. Nature 374:258–262.
Burden, S. J., Sargent, P. B., and McMahan, U. J. (1979). Acetylcholine receptors in regenerating muscle accumulate at original synaptic sites in the absence of the nerve. J. Cell Biol. 82:412–425.
McMahan, U. J., and Slater, C. R. (1984). The influence of basal lamina on the accumulation of acetylcholine receptors at synaptic sites in regenerating muscle. J. Cell Biol. 98:1453–1473.
Ruegg, M. A., Tsim, K. W. K., Horton, S. E., Kroger, S., Escher, G., Gensch, E. M., and McMahan, U. J. (1992). The agrin gene codes for a family of basal lamina proteins that differ in function and distribution. Neuron 8:691–699.
Tsim, K. W. K., Ruegg, M. A., Escher, G., Kroger, S., and McMahan, U. J. (1992). cDNA that encodes active agrin. Neuron 8: 677–689.
Rupp, F., Payan, D. G., Magill-Solc, C., Cowan, D. M., and Serieller, R. H. (1991). Structure and expression of a rat agrin. Neuron 6:811–823.
Ferns, M., Hoch, W., Campanelli, J. T., Rupp, F., Hall, Z. W., and Serieller, R. H. (1992). RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes. Neuron 8:1079–1086.
Hoch, W., Ferns, M., Campanelli, J. T., Hall, Z. W., and Serieller, R. H. (1993). Developmental regulation of highly active alternatively spliced forms of agrin. Neuron 11:479–490.
Ferns, M. J., Campanelli, J. T., Hoch, W., Scheller, R. H., and Hall, Z. W. (1993). The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron 11: 491–502.
Nitkin, R. M., Smith, M. A., Magill, C., Fallon, J. R., Yao, Y.-M. M., Wallace, B. G., and McMahan, U. J. (1987). Identification of agrin, a synaptic organizing protein from Torpedo electric organ. J. Cell Biol. 105:2471–2478.
Magill-Solc, C., and McMahan, U. J. (1988). Motor neurons contain agrin-like molecules. J. Cell Biol. 107:1825–1833.
Reist, N. E., Werle, M. J., and McMahan, U. J. (1992). Agrin released by motor neurons induces the aggregation of acetylcholine receptors at neuromuscular junctions. Neuron, 8:865–868.
Cohen, M. W., and Godfrey, E. W. (1992). Early appearance of and neuronal contribution to agrin-like molecules at embryonic frog nerve-muscle synapses formed in culture. J. Neurosci. 12:2982–2992.
Tsen, G., Halfter, W., Kroger, S., and Cole, G. J. (1995). Agrin is a heparan sulfate proteoglycan. J. Biol. Chem. 270:3392–3399.
Gee, S. H., Montanaro, F., Lindenbaum, M. H., and Carbonetto, S. (1994). Dystroglycan-α, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 77:675–686.
Bowe, M. A., Deyst, K. A., Leszyk, J. D., and Fallon, J. R. (1994). Identification and purification of an agrin receptor from Torpedo postsynaptic membranes: A heteromeric complex related to the dystroglycans. Neuron 12:1173–1180.
Sugiyama, J., Bowen, D. C., and Hall, Z. W. (1994). Dystroglycan binds nerve and muscle agrin. Neuron 13:1–20.
Singer, S. J., and Nicholson, G. L. (1972). The fluid mosaic model of the structure of cell membranes. Science 175:720–731.
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Bloch, R.J. (1996). The Membrane-Associated Cytoskeleton and Exoskeleton. In: Schultz, S.G., Andreoli, T.E., Brown, A.M., Fambrough, D.M., Hoffman, J.F., Welsh, M.J. (eds) Molecular Biology of Membrane Transport Disorders. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1143-0_3
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