Advertisement

Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Focal adhesion as a signal transduction organelle

This is a preview of subscription content, log in to check access.

References

  1. Abercrombie M, Dunn GA: Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp Cell Res 92: 57–62, 1975

  2. Abercrombie M, Heaysman J, Pegrum SM: The locomotion of fibroblasts in culture. Exp Cell Res 67: 359–367, 1971

  3. Anderson D, Koch CA, Grey L, Ellis C, Moran M, Pawson T: Binding of SH2 domains of phospholipase Cγ1, GAP, and Src to activated growth factor receptors. Science 250: 979–982, 1990

  4. Bao S, Li J, Brucato C, Platz J, Chen LB: Molecular cloning and sequencing of a novel 55/60 kD focal contact protein. Mol Bio Cell 3: 70a, 1992

  5. Beckerle MC: The adhesion plaque protein, talin, is phosphorylatedin vivo in chicken embryo fibroblasts exposed to a tumorpromoting phorbol ester. Cell Reg 1: 227–236, 1990

  6. Bresnick AR, Janmey PA, Condeelis J: Evidence that a 27-residue sequence is the actin-binding site of ABP-120. J Biol Chem 266: 12989–12993, 1991

  7. Bresnick AR, Warren V, Condeelis J: Identification of a short sequence essential for actin binding by Dictyostelium ABP-120. J Biol Chem 265: 9236–9240, 1990

  8. Bretscher A: Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J Cell Biol 108: 921–930, 1989

  9. Brugge JS, Erikson RL: Identification of a transformation-specific antigen induced by avian sarcoma virus. Nature 269: 346–348, 1977

  10. Burridge K, Connell L: A new protein of adhesion plaques and ruffling membranes. J Cell Biol 97: 359–367, 1983

  11. Burridge K, Fath K, Kelly T, Nuckolls G, Turner C: Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 4: 487–525, 1988

  12. Burridge K, Mangeat P: An interaction between vinculin and talin. Nature 308: 744–746, 1984

  13. Burridge K, Turner C, Romer L: Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 119: 893–904, 1992

  14. Camilli P, Benfenati F, Valtorta F, Greengard P: The synapsins. Annu Rev Cell Biol 6: 433–460, 1990

  15. Cantor C, Schimmel P: Biophysical Chemistry. New York, W.H. Freeman.: p 561, 1980

  16. Chen WT: Membrane proteases: roles in tissue remodeling and tumour invasion. Curr Opin Cell Biol 4: 802–809, 1992

  17. Chen WT, Chen JM, Mueller SC: Coupled expression and colocalization of 140K cell adhesion molecules, fibronectin, and laminin during morphogenesis and cytodifferentiation of chick lung cells. J Cell Biol 103: 1073–1090, 1986

  18. Chen WT, Olden K, Bernard BA, Chu F: Expression of transformation-associated protease(s) that degrade fibronectin at cell contact site. J Cell Biol 98: 1546–1555, 1984

  19. Cooper JA: Effects of cytochalasin and phalloidin on actin. J Cell Biol 105: 1473–1478, 1987

  20. Cooper JA, Bryan J, Schwab B, Frieden C, Loftus DJ, Elson EL: Microinjection of gelsolin into living cells. J Cell Biol 105: 491–501, 1987

  21. Crawford AW, Beckerle MC: Purification and characterization of zyxin, an 82,000-Dalton component of adherens junctions. J Biol Chem 266: 5847–5853, 1991

  22. D'Andrea AD, Fasman GD, Londish HF: Erythropoietin receptor and interleukin-2 receptor beta chain: a new receptor family. Cell 58: 1023–1024, 1989

  23. Davis S, Lu ML, Lo SH, Lin S, Butler JA, Druker BJ, Roberts TM, An Q, Chen LB: Presence of an SH2 domain in the actinbinding protein tensin. Science 252: 712–715, 1991

  24. DeClue JE, Martin GS: Phosphorylation of talin at tyrosine in Rous sarcoma virus-transformed cells. Mol Cell Biol 7: 371–378, 1987

  25. DeClue JE, Martin S: Linker insertion-deletion mutagenesis of the v-Src gene: isolation of host and temperature-dependent mutants. J Virol 63: 542–554, 1989

  26. DeClue JE, Sadowski I, Martin GS, Pawson TA: A conserved domain regulates interactions of the v-fps protein-tyrosine kinase with the host cell. Proc Natl Acad Sci USA 84: 9064–9068, 1987

  27. Diamond L, O'Brien TC, Baird WM: Tumor promoters and the mechanism of tumor promotion. Adv Cancer Res 32: 1–74, 1980

  28. Drubin DG, Mulholland J, Zhu Z, Botstein D: Homology of a yeast actin-binding protein to signal transduction proteins and myosin-I. Nature 343: 288–290, 1990

  29. Evans RR, Robson RM, Stromer MH: Properties of smooth muscle vinculin. J Biol Chem 259: 3916–3924, 1984

  30. Fantl WJ, Escobedo JA, Martin AG, Turck CW, Rosario MD, McCormick F, Williams LT: Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 69: 413–423, 1992

  31. Feramisco JR, Burridge K: A rapid purification of α-actinin, filamin, and a 130,000-Dalton protein from smooth muscle. J Biol Chem 255: 1194–1199, 1980

  32. Frixen UH, Behrens M, Sachs M, Eberle G, Voss B, Warda A, Lochner D, Birchmeir W: E-cadherin-mediated cell-cell adhesion prevents invasiveness of human carcinoma cells. J Cell Biol 113: 173–185, 1991

  33. Fuchtbauer A, Jockusch BM, Maruta H, Kilimann MW, Isenberg G: Disruption of microfilament organization after injection of F-actin capping proteins into living tissue culture cells. Nature 304: 361–364, 1983

  34. Gaertner A, Wegner A: Mechanism of the insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin. J Muscle Res Cell Mot 12: 27–36, 1991

  35. Geiger B: A 130k protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18: 193–205, 1979

  36. Geiger B, Avnur Z, Kreis TE, Schlessinger J: The dynamics of cytoskeletal organization in areas of cell contact. Cell Muscle Motil 5: 195–234, 1984

  37. Geiger B, Ginsberg D, Salomon D, Volborg T: The molecular basis for the assembly and modulation of adherens-type junctions. Cell Differen Develop 32: 343–354, 1990

  38. Giancotti FG, Ruoslahti E: Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese Hamster Ovary Cells. Cell 60: 849–859, 1990

  39. Glenney J, Zokas L: Novel tyrosine kinase substrates from Rous Sarcoma Virus-transformed cells are present in the membrane skeleton. J Cell Biol 108: 2401–2408, 1989

  40. Gluck U, Kwiatkowski DJ, Ben-Ze'ev A: Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells transfected with α-actinin cDNA. Proc Natl Acad Sci USA 90: 383–387, 1993

  41. Godman G, Miranda A: Cellular contractility and the visible effects of cytochalasin. Amsterdam, Elsevier/North Holland, 1978

  42. Grinnell F: Focal adhesion sites and the removal of substratumbound fibronectin. J Cell Biol 103: 2697–2706, 1986

  43. Guan J, Shalloway D: Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358: 690–692, 1992

  44. Hartwig JH, Kwiatkowski O: Actin-binding proteins. Curr Opin Cell Biol 3: 87–97, 1991

  45. Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A: MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium calmodulin. Nature 356: 618–622, 1992

  46. Hatakeyama M, Kono T, Kobayashi N, Kawahara A, Levin S, Perlumutter RM, Taniguchi T: Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association. Science 252: 1523–1528, 1991

  47. Herman B, Pledger WJ: Platelet-derived growth factor-induced alterations in vinculin and actin distribution in BALB/c/3T3 cells. J Cell Biol 100: 1031–1040, 1985

  48. Hirai H, Varmus HE: Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol Cell Biol 10: 1307–1318, 1990

  49. Hirono M, Tanaka R, Watanabe Y: Tetrahymena actin: copolymerization with skeletal muscle actin interactions with muscle actin-binding proteins. J Biochem 107: 32–36, 1990

  50. Hirst R, Horwitz A, Buck C, Rohrschneider L: Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encodes tyrosine kinases. Proc Natl Acad Sci USA 83: 6470–6474, 1986

  51. Holmes KC, Popp D, Gebhard W, Kabsch W: Atomic model of the actin filament. Nature 347: 44–49, 1990

  52. Horwitz A, Bozyczko D, Buck CA: The integrin family and neighbors. New York, John Wiley & Sons, 1990

  53. Horwitz A, Duggen K, Buck C, Beckerle MC, Burridge K: Interactions of plasma membrane fibronectin receptors with talin-a transmembrane linkage. Nature 320: 531–533, 1986

  54. Hunter T: Protein modification: phosphorylation on tyrosine residues. Curr Opin Cell Biol, 1989

  55. Hunter T, Sefton BM: The transforming gene product of Rous sarcoma virus phosphoryates tyrosine. Proc Natl Acad Sci USA 77: 1311–1315, 1980

  56. Hynes RO: Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11–25, 1992

  57. Jaken S, Leach K, Klauck LR: Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts. J Cell Biol 109: 687–704, 1989

  58. Janmey PA, Peetermans J, Zaner KS, Stossel TP, Tanaka T: Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry, and electron microscopy. J Biol Chem 261: 8357–8362, 1986

  59. Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC: Atomic structure of the actin: DNase I complex. Nature 347: 37–44, 1990

  60. Kanner SB, Reynolds AB, Vines RR, Parsons JT: Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 87: 3328–3332, 1990

  61. Kashishian A, Kazlauskas A, Cooper JA: Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinasein vivo. EMBO J 11: 1373–1382, 1992

  62. Kaufmann S, Kas J, Doldmann WH, Sackmann E, Isenberg G: Talin anchors and nucleates actin filaments at lipid membranes: a direct demonstration. FEBS Letters 314: 203–205, 1992

  63. Kaufmann S, Piekenbrock T, Goldmann WH, Barmann M, Isenberg G: Talin binds to actin and promotes filament nucleation. FEBS 284: 187–191, 1991

  64. Kawamoto S, Hidaka H: Ca2+-activated, phospholipid-dependent protein kinase catalyzes the phosphorylation of actinbinding proteins. Biochem Biophys Res Commun 118: 736–742, 1984

  65. Kellie S: Cellular transformation, tyrosine kinase, and the cellular adhesion plaque. BioAssays 8: 25–30, 1988

  66. Kellie S, Holme TC, Bissell MJ: Interaction of tumor promoters with epithelial cells in culture: an immunofluorescence study. Exp Cell Res 160: 259–274, 1985

  67. Kitamura T, Hayashida K, Sakamaki K, Yokota T, Arai K, Miyajima A: Reconstitution of functional human granulocyte/macrophage colony-stimulating factor (GM-CSF): evidence that AIC2B is a subunit of murine GM-CSF receptor. Proc Natl Acad Sci USA 88: 5082–5086, 1991

  68. Kitamura T, Sato N, Arai K-I, Miyajima A: Expression cloning of the human IL-3 receptor cDNA reveals a shared β subunit for the human IL-3 and GM-CSF receptors. Cell 66: 1165–1174, 1991

  69. Koch CA, Anderson D, Moran F, Ellis C, Pawson T: SH2 and SH3 domains: elements that control ineractions of cytoplasmic signaling proteins. Science 252: 668–674, 1991

  70. Kouyama T, Mihashi K: Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114: 33–38, 1981

  71. Kramarcy NR, Sealock R: 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, 1990

  72. Kreis TE, Geiger D, Schlessinger J: Mobility of microinjected rhodamine actin within living chicken gizzard cells determined by fluorescence photobleaching recovery. Cell 29: 835–845, 1982

  73. Lazarides E, Burridge K: α-Actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell 6: 289–298, 1975

  74. Linnekin D, Evans GA, D'Andrea A, Farrar WL: Association of erythropoietin receptor with protein tyrosine kinase activity. Proc Natl Acad Sci USA 89: 6237–6241, 1992

  75. Lo SH, Chen LB: Phosphorylation of tensin. In preparation, 1993a

  76. Lo SH, Chen LB: Tensin has tumor suppression activity. In preparation, 1993b

  77. Lo SH, Janmey P, Hartwig J, Chen LB: Tensin, an SH2 domain-containing protein, has multiple actin-binding domains. Submitted, 1993

  78. Luna EJ, Hitt AL: Cytoskeleton-plasma membrane interactions. Science 258: 955–964, 1992

  79. Maher PA, Pasquale EB, Wang JY, Singer SJ: Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc Natl Acad Sci USA 82: 6576–6580, 1985

  80. Margolis B: Protein with SH2 domains: transducers in the tyrosine kinase signaling pathway. Cell Growth & Differ 3: 73–80, 1992

  81. Matsuda M, Mayer BJ, Hanafusa H: Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins. Mol Cell Biol 11(3): 1607–1613, 1991

  82. Matsudaira P: Modular organization of actin crosslinking proteins. Trends Biochem Sci 16: 87–92, 1991

  83. Mayer B, Hanafusa H: Association of the v-crk oncogene product with phosphotyrosine containing proteins and protein kinase activity. Proc Natl Acad Sci USA 87: 2638–1642, 1990

  84. Mayer BJ, Jackson P, Baltimore D: The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc Natl Acad Sci USA 88: 627–631, 1991

  85. Meige JB, Wang YL: Reorganization of α-actinin and vinculin induced by a phorbol ester in living cells. J Cell Biol 102: 1430–1438, 1986

  86. Milligan RA, Whittaker M, Safer D: Molecular structure of Factin and location of surface binding sites. Nature 384: 217–221, 1990

  87. Miron T, Vancompernolle K, Vandekerckhove J, Wilcheck M, Geiger B: A 25-kD inhihitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol 114: 255–261, 1991

  88. Miron T, Wilchek M, Geiger B: Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle. Eur J Biochem 178: 543–553, 1988

  89. Mitchison T: Compare and contrast actin filaments and microtubules. Mol Biol Cell 3: 1309–1315, 1992

  90. Moreno S, Nurse P: Substrates for p34cdc2: in vivo veritas? Cell 61: 549–551, 1990

  91. Muguruma M, Matsumura S, Fukazawa T: Direct interactions between talin and actin. Biochem Biophys Res Commun 171: 1217–1223, 1990

  92. Nagafuchi A, Takeichi M, Tsukita S: The 102 kD cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression. Cell 65: 849–857, 1991

  93. Navarro PM, Gomez A, Pizarro A, Gamallo C, Quintanilla M, Cano A: A role for the E-cadherin cell-cell adhesion molecule during tumor progression of mouse epidermal carcinogenesis. J Cell Biol 115: 517–533, 1991

  94. Nemeth SP, Fox LG, DeMarco M, Brugge J: Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein. Mol Cell Biol 9: 1109–1119, 1989

  95. Nishizuka Y: Turnover of inositol phospholipids and signal transduction. Science 225: 1365–1370, 1984

  96. Nurse P: Universal control mechanism regulating onset of Mphase. Nature 344: 503–508, 1990

  97. O'Brien MC, Fukui Y, Hunafusa H: Activation of the protooncogene p60src by point mutations in the SH2 domain. Mol Cell Biol 10: 2855–2862, 1990

  98. Otey CA, Pavalko FM, Burridge K: An interaction between α-actinin and β1 integrin subunitin vitro. J Cell Biol 111: 721–729, 1990

  99. Pasquale EB, Maher PA, Singer SJ: Talin is phosphorylated on tyrosine in chicken embryo fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sci USA 83: 5507–5511, 1986

  100. Pavalko FM, Otey CA, Burridge K: Identification of a filamin isoform enriched at the end of stress fibers in chicken fibroblasts. J Cell Sci: 109-118, 1989

  101. Pawson T, Gish GD: SH2 and SH3 domains: domains from structure to function. Cell 71: 359–362, 1992

  102. Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON: BCR sequences essential for transformation by the BCRABL oncogene bind to the ABL src-homology-2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell 66: 161, 1991

  103. Reinhard M, Halbrugge M, Scheer U, Wiegand C, Jockusch BM, Walter U: The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J 11: 2063–2070, 1992

  104. Ridley AJ, Hall A: The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70: 389–399, 1992

  105. Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A: The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401–410, 1992

  106. Rocco M, Carson M, Hantgan R, McDonagh J, Hermans J: Dependence of the shape of the plasma fibronectin molecule on solvent composition. Ionic strength and glycerol content. J Biol Chem 258: 14545–14549, 1983

  107. Rodriguez-Fernandez JL, Geiger B, Salomon D, Sabanay I, Zoller M, Ben-Ze'ev A: Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA. J Cell Biol 119: 427–438, 1992

  108. Rohrschneider LR: Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc Natl Acad Sci USA 77: 3514–3518, 1980

  109. Rohrschneider LR, Rosok MJ: Transformation parameters and pp60src localization in cells infected with partial transformation mutants of Rous sarcoma virus. Mol Cell Biol 3: 731–746, 1983

  110. Rosen A, Keenan KF, Thelen M, Nairn AC, Aderem A: Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. J Exp Med 172: 1211–1215, 1990

  111. Ruhnau K, Gaertner A, Wegner A: Kinetic evidence for insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin, a protein purified from smooth muscle. J Mol Biol 210: 141–148, 1989

  112. Sadler I, Crawford AW, Michelsen JW, Beckerle MC: Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. J Cell Biol 119: 1573–1587, 1992

  113. Sadowski I, Stone JC, Pawson TA: A non-catalytic domain conserved among cytoplasmic protein-tyrosine modifies the kinase function and transforming activity of Fujinami sarcoma virus p130gag-fps. Mol Cell Biol 6: 4396–4408, 1986

  114. Sato N, Funayama N, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S: A gene family consisting of ezrin, radixin and moesin. Its specific localization of actin filament/plasma membrane association sites. J Cell Sci 103: 131–143, 1992

  115. Sato N, Yonemura S, Obinata T, Tsukita S, Tsukita S: Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis. J Cell Biol 113(2): 321–330, 1991

  116. Schaller MD, Borgman CA, Cobb BS, Vines RR, Reynolds AB, Parsons JT: pp125FAK, a structurally distinctive protein tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci USA 89: 5192–5196, 1992

  117. Schaller MD, Borgman CA, Parsons JT: Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. Mol Cell Biol 13: 785–791, 1993

  118. Schlessinger J, Geiger B: Epidermal growth factor induces redistribution of actin and α-actinin in human epidermal carcinoma cells. Exp Cell Res 134: 273–279, 1981

  119. Schliwa M, Nakamura T, Porter KR, Euteneuer V: A tumor promoter induces rapid and coordinated reorganization of actin and vinculin in cultured cells. J Cell Biol 99: 1045–1059, 1984

  120. Schroer E, Wegner A: Purification and characterization of a protein from chicken gizzard, which inhibits actin polymerization. Eur J Biochem 153: 515–520, 1985

  121. Schwartz MA, Both G, Lechene C: Effect of cell spreading on cytoplasmic pH in normal and transformed fibroblasts. Proc Natl Acad Sci USA 86: 4525–4529, 1989

  122. Schwartz MA, Ingber DE, Lawrence M, Sringer TA, Lechene C: Multiple integrins share the ability to induce elevation of intracellular pH. Exp Cell Res 195: 533–535, 1991

  123. Schwartz MA, Rupp EE, Frangioni JV, Lechene C: Cytoplasmic pH and anchorage-independent growth induced by v-Ki-ras, v-src or polyoma middle T. Oncogene 5: 55–58, 1990

  124. Sefton BM, Hunter T, Ball EH, Singer SJ: Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 24: 165–174, 1981

  125. Small JV: The actin cytoskeleton. Electron Microsc Rev 1: 155–174, 1988

  126. Songyang Z, Shoelson SE, Chaudhuri M, Gish C, Pawson T, Haser WG, King F, Roberts T, Ratnofsky S, Lechleider RJ, Neel BG, Birge RB, Fajardo JE, Chou MM, Hanafusa H, Schaffhausen B, Cantley LC: SH2 domains recognize specific phosphopeptide sequences. Cell 72: 767–778, 1993

  127. Trofatter JAet al.: A novel moesin-, ezrin-, radixin-like gene is a candidate for the neurofibromatosis 2 tumor suppressor. Cell 72: 791–800, 1993

  128. Tsukita S, Itoh M, Tsukita S: A new 400-kD protein from isolated adherens junctions: its localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles. J Cell Biol 109: 2905–2915, 1989

  129. Turner C: Paxillin is a major phosphotyrosine-containing protein during embryonic development. J Cell Biol 115: 201–207, 1991

  130. Turner CE, Burridge K: Transmembrane molecular assemblies in cell-extracellular matrix interactions. Cur Opin Cell Biol 3: 849–853, 1991

  131. Turner CE, Glenney JR, Burridge K: Paxillin: A new vinculin-binding protein present in focal adhesions. J Cell Biol 111: 1059–1068, 1990

  132. Turner CE, Pavalko FM, Burridge K: The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity. J Biol Chem 264: 11938–11944, 1989

  133. Vleminckx K, Vakaet L, Mareel M, Fiers W, Van Roy F: Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell 66: 107–119, 1991

  134. Walsh TP, Weber A, Higgins J, Bonder EM, Mooseker MS: Effect of villin on the kinetics of actin polymerization. Biochemistry 23: 2613–2621, 1984

  135. Wang H-CR, Parsons JT: Deletions and insertions with an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stability. J Virol 63: 291–302, 1989

  136. Wang Y-L: Reorganization of actin filament bundles in living fibroblasts. J Cell Biol 99: 1478–1485, 1984

  137. Weigt C, Gaertner A, Wegner A, Korte H, Meyer HE: Occurrence of an actin-inserting domain in tensin. J Mol Biol 227: 593–595, 1992

  138. Werth DK, Niedel JE, Pastan I: Vinculin, a cytoskeletal substrate for protein kinase C. J Biol Chem 258: 11423–11426, 1983

  139. Wilkins JA, Lin S: A re-examination of the interaction of vinculin with actin. J Cell Biol 102: 1085–1092, 1986

  140. Wilkins JA, Lin S: High affinity interaction of vinculin with actin filamentsin vitro. Cell 28: 83–90, 1982

  141. Wilkins JA, Risinger MA, Coffey E, Lin S: Purification of a vinculin binding protein from smooth muscle. J Cell Biol 104: 130a, 1987

  142. Williams EC, Janmey PA, Ferry JD, Mosher DF: Conformational states of fibronectin. Effects of pH, ionic strength, and collagen binding. J Biol Chem 257: 14973–14978, 1982

  143. Woods A, Couchman JR: Protein kinase C involvement in focal adhesion formation. J Cell Sci 101: 277–290, 1992

Download references

Author information

Correspondence to Lan Bo Chen.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Lo, S.H., Chen, L.B. Focal adhesion as a signal transduction organelle. Cancer Metast Rev 13, 9–24 (1994). https://doi.org/10.1007/BF00690415

Download citation

Key words

  • focal adhesion
  • signal transduction organelle