Abstract
Eukaryotic cells are compartmentalized, increasing the efficiency of the cell by allowing the existence of microenvironments of unique properties and by segregating potentially incompatible biochemical reactions. The targeting of newly synthesized macromolecules to their correct location within the cell and the maintenance of the distinctive macromolecular composition of these compartments is an important feature of cellular organization. The mechanisms by which cells direct the intracellular traffic of macromolecules are the subject of much investigation in cell biology. One well-studied example of intracellular sorting and trafficking is the mannose 6-phosphate-mediated transport of lysosomal enzymes.
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Bishop, D.F., Calhoun, D.H., Bernstein, H.S., Hantzopoulos, P., Quinn, M., and Desnick, R. J., 1986, Human a-galactosidase A: Nucleotide sequence of a eDNA clone encoding the mature enzyme, Proc. Natl. Acad. Sei. USA, 83: 4859–4863.
Brown, W.J., Constantinescu, E., and Farquhar, M.G., 1984, Redistribution of mannose 6-phosphate receptors induced by tunicamycin and chloroquine, J. Cell Biol., 99: 320–326.
Brown, W.J., and Farquhar, M.G., 1984, The mannose 6-phosphate receptor for lysosomal enzymes is concentrated in cis Golgi cisternae, Cell, 36: 295–307.
Brown, W.J., Goodhouse, J., and Farquhar, M.G., 1986, Mannose 6-phosphate receptors for lysosomal enzymes cycle between the Golgi complex and endosomes, J. Cell Biol., 103: 1235–1247.
Creek, K.E., Grubb, J.H., and Sly, W.S., 1983 Immunological inactivation of receptor-mediated uptake and intracellular sorting of lysosomal enzymes, J. Cell Biol., 97:253a (abstract).
Creek, K.E., and Sly, W.S., 1983, Biosynthesis and turnover of the phospho- mannosyl receptor in human fibroblasts, Biochem. J., 214: 353–360.
Creek, K.E., and Sly, W.S., 1984, The role of the phosphomannosyl receptor in the transport of acid hydrolases to lysosomes, in: “Lysosomes in Biology and Pathology,” J.T. Dingle, R.T. Dean, and W.S. Sly, eds., Elsevier, Amsterdam.
De Duve, C., De Barsy, T., Poole, B., Trouet, A., Tulkens, P., and van Hoof, F., 1974, Lysosomotropic agents, Biochem. Pharmacol., 23: 2495–2531.
Dunphy, W.G., Fries, E., Urbani, L.J., and Rothman, J.E., 1981, Early and late functions associated with the Golgi apparatus reside in distinct compartments, Proc. Natl. Acad. Sci. USA, 78:7453–7457.
Faust, P.L., Kornfeld, S., and Chirgwin, J.M., 1985, Cloning and sequence analysis of eDNA for human cathepsin D, Proc. Natl. Acad. Sci. USA, 82: 4910–4914.
Fedde, K.N., and Sly, W.S., 1985, Ricin-binding properties of acid hydrolases from isolated lysosomes implies prior processing by terminal transferases of the trans-Golgi apparatus, Biochem. Biophys. Res. Commun., 133: 614–620.
Fischer, H.D., Gonzalez-Noriega, A., and Sly, W.S., 1980a, 8-glucuronidase binding to human fibroblast membrane receptors, J. Biol. Chem., 255: 5069–5074.
Fischer, H.D., Gonzalez-Noriega, A., Sly, W.S., and Morre, D.J., 1980b, Phosphomannosyl-enzyme receptors in rat liver, J. Biol. Chem., 255: 9608–9615.
Fischer, H.D., Natowicz, M., Sly, W.S., and Bretthauer, R.K., 1980e, Fibroblast receptor for lysosomal enzymes mediates pinocytosis of multivalent phosphomannan fragment, J. Cell Biol., 84: 77–86.
Freeze, H.H., Miller, A.L., and Kaplan, A., 1980, Acid hydrolases from Dictyostelium discoideum contain phosphomannosyl recognition markers, J. Biol. Chem., 255:11081–11084.
Fukushima, H., de Wet, J.R., and O’Brien, J.S., 1985, Molecular cloning of a eDNA for human a-L-fucosidase, Proc. Natl. Acad. Sci. USA, 82: 1262–1265.
Gabel, C.A., Costello, C.E., Reinhold, V.N., Kurtz, L., and Kornfeld, S., 1984, Identification of methyiphosphomannosyl residues as components of the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins, J. Biol. Chem., 259: 13762–13769.
Gartung, C., Braulke, T., Hasilik, A., and von Figura, K., 1985, Internalization of blocking antibodies against mannose 6-phosphate specific receptors, EMBO J., 4: 1725–1730.
Geuze, H.J., Slot, J.W., Strous, G.J.A.M., Hasilik, A., and von Figura, K., 1984, Ultrastructural localization of the mannose 6-phosphate receptor in rat liver, J. Cell Biol., 98: 2045–2054.
Geuze, H.J., Slot, J.W., Strous, G.J.A.M., Hasilik, A., and von Figura, K., 1985, Possible pathways for lysosomal enzyme delivery, J. Cell Biol., 101: 2253–2262.
Geuze, H.J., Slot, J.W., Strous, G.J.A.M., Lodish, H.F., and Schwartz, A.L., 1983, Intracellular site of asialoglycoprotein receptor-ligand uncoupling: double-labeling immunoelectron microscopy during receptor-mediated endocytosis, Cell, 32: 277–287.
Goldberg, D., Gabel, C., and Kornfeld, S., 1984, Processing of lysosomal enzyme oligosaccharide units, in: “Lysosomes in Biology and Pathology,” J.T. Dingle, R.T. Dean, and W.S. Sly, eds., Elsevier Press, New York.
Goldberg, D.E., and Kornfeld, S., 1981, The phosphorylation of 0-glucuronidase oligosaceharides in mouse P388D1 cells, J. Biol. Chem., 256: 13060–13067.
Goldberg, D.E., and Kornfeld, S., 1983, Evidence for extensive subcellular organization of asparagine-linked oligosaccharide processing and lysosomal enzyme phosphorylation, J. Biol. Chem., 258: 3159–3165.
Gonzalez-Noriega, A., Grubb, J.H., Talkad, V., and Sly, W.S., 1980, Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling, J. Cell Biol., 85: 839–852.
Hasilik, A., Klein, U., Waheed, A., Strecker, G., and von Figura, K., 1980, Phosphorylated oligosaceharides in lysosomal enzymes: Identification of a -N-acetylglucosamine(1)phospho(6)mannose diester groups, Proc. Natl. Acad. Sci. USA, 77: 7074–7078.
Hasilik, A., and Neufeld, E.F., 1980, Biosynthesis of lysosomal enzymes in fibroblasts, J. Biol. Chem., 255: 4937–4945.
Hasilik, A., and von Figura, K., 1984, Processing of lysosomal enzymes in fibroblasts, in: “Lysosomes in Biology and Pathology,” J.T. Dingle, R.T. Dean, and W.S. Sly, eds., Elsevier, Amsterdam.
Hickman, S., and Neufeld, E.F., 1972, A hypothesis for I-cell disease: Defective hydrolases that do not enter lysosomes, Biochem. Biophys. Res. Commun., 49: 992–999.
Hoflack, B., and Kornfeld, S., 1985a, Lysosomal enzyme binding the mouse P388D1 macrophage membranes lacking the 215-kDa mannose 6-phosphate receptor: Evidence for the existence of a second mannose 6-phosphate receptor, Proc. Natl. Acad. Sci. USA, 82: 4428–4432.
Hoflack, B., and Kornfeld, S., 1985b, Purification and characterization of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver, J. Biol. Chem., 260: 12008–12014.
Kaplan, A., Achord, D.T., and Sly, W.S., 1977, Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts, Proc. Natl. Acad. Sei. USA, 74: 2026–2030.
Korneluk, R.G., Mahuran, D.J., Neote, K., Klavins, M.H., O’Dowd, B.F., Tropak, M., Willard, H.F., Anderson, M.J., Lowden, J.A., and Gravel, R.A., 1986, Isolation of eDNA clones coding for the a subunit of human ß-hexo-saminidase, J. Biol. Chem., 261: 8407–8413.
Kornfeld, R., and Kornfeld, S., 1985, Assembly of asparagine-linked oligosaccharides, Ann. Rev. Biochem., 54: 631–664.
Lang, L., Reitman, M.L., Tang, J., Roberts, R.M., and Kornfeld, S., 1984, Lysosomal enzyme phosphorylation, J. Biol. Chem., 259: 14663–14667.
Lemansky, P., Gieselmann, V., Hasilik, A., and von Figura, K., 1985, Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblasts, J. Biol. Chem., 260: 9023–9030.
McKusick, V.A., and Neufeld, E.F., 1983, The mucopolysaccharide storage diseases, in: “The Metabolic Basis of Inherited Disease,” fifth edition, J.B. Stanbury, J.B. Wyngaarden, D.S. Frederickson, J.L. Goldstein, and M.S. Brown, eds., McGraw-Hill, New York.
Mitchell, D.C., Maler, T., and Jourdian, G.W., 1984, Detergent dissociation of bovine liver phosphomannosyl binding protein, J. Cell. Biochem., 24: 319–330.
Myerowitz, R., Piekarz, R., Neufeld, E.F., Shows, T.B., and Suzuki, K., 1985, Human ß-hexosaminidase a chain: Coding sequence and homology with the ß chain, Proc. Natl. Acad. Sci. USA, 82: 7830–7834.
Nishimura, Y., Rosenfeld, M.G., Kreibich, G., Gubler, U., Sabatini, D.D., Adesnik, M., and Andy, R., 1986, Nucleotide sequence of rat preputial gland ß-glueuronidase eDNA and in vitro insertion of its encoded polypeptide into microsomal membranes, Proc. Natl. Acad. Sci. USA, 83: 7292–7296.
Ohkuma, S., and Poole, B., 1978, Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents, Proc. Natl. Acad. Sei. USA, 75: 3327–3331.
Oshima, A., Kyle, J.W., Miller, R.D., Hoffmann, J.W., Powell, P.P., Grubb, J.H., Sly, W.S., Tropak, M., Guise, K.S., and Gravel, R.A., 1987, Cloning, sequencing, and expression of cDNA for human -glucuronidase, Proc. Natl. Acad. Sci. USA, 84: 685–689.
Owada, M., and Neufeld, E.F., 1982, Is there a mechanism for introducing acid hydrolases into liver lysosomes that is independent of mannose 6-phosphate recognition? Mechem. Biophys. Res. Commun., 105: 814–820.
Pohlmann, R., Waheed, A., Hasilik, A., and von Figura, K., 1982, Synthesis of phosphorylated recognition marker in lysosomal enzymes is located in the cis part of Golgi apparatus, J. Biol. Chem., 257: 5323–5325.
Reitman, M.L., and Kornfeld, S., 1981, UDP-N-Acetylglucosamine: Glycoprotein N-acetylglucosamine-1-phosphotransferase, J. Biol. Chem., 256: 4275–4281.
Reitman, A.L., Varki, A., and Kornfeld, S., 1981, Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5’-diphosphate-N-acetylglucosamine: Glycoprotein N-acetylglucosaminylphosphotransferase activity, J. Clin. Invest., 67: 1574–1579.
Robbins, A.R., Peng, S.S., and Marshall, J.L., 1983, Mutant Chinese hamster ovary cells pleiotropically defective in receptor-mediated endocytosis, J. Cell. Biol., 96: 1064–1071.
Rome, L.H., Weissman, B., and Neufeld, E.F., 1979, Direct demonstration of binding of a lysosomal enzyme, a-L-iduronidase, to receptors in cultured fibroblasts, Proc. Natl. Acad. Sci. USA, 76: 2331–2334.
Roth, J., and Berger, E.G., 1982, Immunocytochemical localization of galactosyltransferase in HeLa cells: Codistribution with thiamine pyrophosphatase in trans-Golgi cisternae, J. Cell Biol., 93: 223–229.
Sahagian, G.G., Distler, J., and Jourdian, G.W., 1981, Characterization of a membrane-associated receptor from bovine liver that binds phosphomannosyl residues of bovine testicular ß-galactosidase, Proc. Natl. Acad. Sci. USA, 78: 4289–4293.
Sahagian, G.G., Distler, J., and Jourdian, G.W., 1982, Membrane receptor for phosphomannosyl residues, Methods Enzymol., 83: 392–396.
Sahagian, G.G., and Neufeld, E.F., 1983, Biosynthesis and turnover of the mannose 6-phosphate receptor in cultured Chinese hamster ovary cells, J. Biol. Chem., 257: 7121–7128.
Sahagian, G.G., and Steer, C.J., 1985, Transmembrane orientation of the mannose 6-phosphate receptor in isolated clathrin-coated vesicles, J. Biol. Chem., 260: 9838–9842.
Sly, W.S., Fischer, H.D., Gonzalez-Noriega, A., Grubb, J.H., and Natowicz, M., 1981, Role of the 6-phosphomannosyl-enzyme receptor in intracellular transport and adsorptive pinocytosis of lysosomal enzymes, in: “Basic Mechanisms of Cellular Secretion,” A.R. Hand and C. Oliver, eds., Academic Press, New York.
Sly, W.S., Merion, M., Schlesinger, P., Moehring, J.M., and Moehring, T.J., 1983, Defective endosome acidification in mammalian cell mutants “cross-resistant” to certain toxins and viruses, in: “Protein Synthesis,” A.K. Abraham, T.S. Elkhorn, and I.F. Pryme, eds., The Humana Press, Clifton, NJ.
Steiner, A.W., and Rome, L.H., 1982, Assay and purification of a solubilized membrane receptor that binds the lysosomal enzyme a-L-iduronidase, Arch. Biochem. Biophys., 214: 681–687.
Tager, J.M., 1984, Biosynthesis and deficiency of lysosomal enzymes, Trends Biochem. Sci., 10:324–326.
Takahashi, T., Schmidt, P.G., and Tang, J., 1983, Oligosaceharide units of lysosomal cathepsin D from porcine spleen, J. Biol. Chem., 258: 2819–2830.
Tsuji, S., Choudary, P.V., Martin, B.M., Winfield, S., Barranger, J.A., and Ginns, E.J., 1986, Nucleotide sequence of cDNA containing the complete coding sequence for human lysosomal glucocerebrosiolase, J. Biol. Chem., 261: 50–53.
van Elsen, A.F., and Leroy, J.G., 1979, Lysosomal enzymes in fibroblasts: Lectin affinities, in: “Models for the Study of Inborn Errors of Metabolism,” F.A. Hommes, ed., Elsevier/North-Holland Biomedical Press, Amsterdam.
Varki, A., and Kornfeld, S., 1981, Purification and characterization of rat liver a-N-acetylglucosaminyl phosphodiesterase, J. Biol. Chem., 256: 9937–9943.
von Figura, K., Gieselmann, V., and Hasilik, A., 1984, Antibody to mannose 6-phosphate specific receptor induces receptor deficiency in human fibroblasts, EMBO J., 3: 1281–1286.
von Figura, K., Gieselmann, V., and Hasilik, A., 1985, Mannose 6-phosphate specific receptor is a transmembrane protein with a C-terminal extension oriented towards the cytosol, Biochem. J., 225: 543–547.
von Figura, K., and Weber, E., 1978, An alternative hypothesis of cellular transport of lysosomal enzymes in fibroblasts, Biochem. J., 176: 943–950.
Vladutiu, G.D., 1983, Effect of the co-existence of galactosyl and phosphomannosyl residues of ß-hexosaminidase on the processing and transport of the enzyme in MLI fibroblasts, Biochim. Biophysica Acta, 760: 363–370.
Waheed, A., Hasilik, A., and von Figura, K., 1981, Processing of the phosphorylated recognition marker in lysosomal enzymes, J. Biol. Chem., 256: 5717–5721.
Waheed, A., Hasilik, A., and von Figura, K., 1982a, UDP-N-acetylglucosamine: Lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase, J. Biol. Chem., 257:12322–12331.
Waheed, A., Pohlmann, R., Hasilik, A., von Figura, K., van Elsen, A., and Leroy, J.G., 1982b, Deficiency of UDP-N-acetylglucosamine: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in organs of I-cell patients, Biochem. Biophys. Res. Commun., 105: 1052–1058.
Walter, P. and Lingappa, V.R., 1986, Mechanism of protein translocation across the endoplasmic reticulum membrane, Ann. Rev. Cell Biol., 2: 499–516
Willingham, M.C., Pastan, I.H., and Sahagian, G.G., 1983, Ultrastructural immunocytochemical localization of the phosphomannosyl receptor in Chinese hamster ovary ( CHO) cells, J. Histochem. Cytochem., 31: 1–11.
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Nolan, C.M., Sly, W.S. (1987). Intracellular Traffic of the Mannose 6-Phosphate Receptor and Its Ligands. In: Atassi, M.Z. (eds) Immunobiology of Proteins and Peptides IV. Advances in Experimental Medicine and Biology, vol 225. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5442-0_17
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