Clathrin: Its Role in Receptor-Mediated Vesicular Transport and Specialized Functions in Neurons

References

• Acton S. L., Brodsky F. M. Predominance of clathrin light chain LCb correlates with the presence of a regulated secretory pathway. J. Cell Biol. 1990; 111: 1419–1426
   Google Scholar
• Ahle S., Mann A., Eichelsbacher U., Ungewickell E. Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane. EMBO J. 1988; 7: 919–929
   PubMedGoogle Scholar
• Ahle S., Ungewickell E. Purification and properties of a new clathrin assembly protein. EMBO J. 1986; 5: 3143–3149
   PubMedGoogle Scholar
• Ahle S., Ungewickell E. Identification of a clathrin binding subunit in the HA2 adaptor protein complex. J. Biol. Chem. 1989; 264: 20089–20093
   PubMedGoogle Scholar
• Ahle S., Ungewickell E. Auxilin, a newly identified clathrin-associated protein in coated vesicles from bovine brain. J. Cell Biol. 1990; 111: 19–29
   Google Scholar
• Anderson R. G. W. Multiple endocytic pathways. J. Invest. Dermatol. 1992; 99: 7S–9S
   Google Scholar
• Anderson R. G. W., Brown M. S., Goldstein J. L. Role of the coated endocytic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts. Cell 1977; 10: 351–364
   PubMed Web of Science ®Google Scholar
• Bar-Zvi D., Branton D. Clathrin-coated vesicles contain two protein kinase activities. J. Biol. Chem. 1986; 261: 9614–9621
   Google Scholar
• Bar-Zvi D., Mosley S. T., Branton D. In vivo phosphorylation of clathrin-coated vesicle proteins from rat reticulocytes. J. Biol. Chem. 1988; 263: 4408–4415
   Google Scholar
• Beck K. A., Chang M., Brodsky F. M., Keen J. H. Clathrin assembly protein AP-2 induces aggregation of membrane vesicles: a possible role for AP-2 in endosome formation. J. Cell Biol 1992; 119: 787–796
   Google Scholar
• Beck K. A., Keen J. H. Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP-2. J. Biol. Chem. 1991a; 266: 4442–4447
   PubMedGoogle Scholar
• Beck K. A., Keen J. H. Self-association of the plasma membrane-associated clathrin assembly protein AP-2. J. Biol. Chem. 1991b; 266: 4437–4441
   Google Scholar
• Black M. M., Chestnut M. H., Pleasure I. T., Keen J. H. Stable clathrin: uncoating protein (hsc70) complexes in intact neurons and their axonal transport. J. Neurosci. 1991; 11: 1163–1172
   PubMed Web of Science ®Google Scholar
• Blank G. S., Brodsky F. M. Site-specific disruption of clathrin assembly produces novel structures. EMBO J. 1986; 5: 2087–2095
   Google Scholar
• Blank G. S., Brodsky F. M. Clathrin assembly involves a light chain-binding region. J. Cell Biol. 1987; 105: 2011–2019
   Google Scholar
• Bleil J. D., Bretscher M. S. Transferrin receptor and its recycling in HeLa cells. EMBO J. 1982; 1: 351–355
   PubMed Web of Science ®Google Scholar
• Bretscher M. S., Thomson J. N., Pearse B. M. F. Coated pits act as molecular filters. Proc. Natl. Acad. Sci. U.S.A. 1980; 77: 4156–4159
   PubMed Web of Science ®Google Scholar
• Brodsky F. M. Living with clathrin: its role in intracellular membrane traffic. Science 1988; 242: 1396–1402
   PubMed Web of Science ®Google Scholar
• Brodsky F. M., Galloway C. J., Blank G. S., Jackson A. P., Seow H.-F., Drickamer K., Parham P. Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity. Nature 1987; 326: 203–205
   Google Scholar
• Brodsky F. M., Hill B. L., Acton S. L., Näthke I., Wong D. H., Ponnambalam S., Parham P. Clathrin light chains: arrays of protein motifs that regulate coated vesicle dynamics. TIBS 1991; 16: 208–213
   Google Scholar
• Brodsky F. M., Parham P. Polymorphism in clathrin light chains from different tissues. J. Mol. Biol. 1983; 167: 197–204
   Google Scholar
• Brown W. J., Farquhar M. G. Accumulation of coated vesicles bearing mannose 6-phosphate receptors for lysosomal enzymes in the Golgi region of I-cell fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 5135–5139
   PubMed Web of Science ®Google Scholar
• Burgess T. L., Kelly R. B. Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 1987; 3: 243–293
   PubMedGoogle Scholar
• Carter L. L., Redelmeier T. E., Woollenweber L. A., Schmid S. L. Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis. J. Cell Biol. 1993; 120: 37–45
   PubMed Web of Science ®Google Scholar
• Chang M. P., Mallet W. G., Mostov K. E., Brodsky F. M. Adaptor self-aggregation, adaptor-receptor recognition and binding of α-adaptin subunits to the plasma membrane contribute to recruitment of adaptor (AP2) components of clathrin-coated pits. EMBO J. 1993; 12: 2169–2180
   Google Scholar
• Chappell T. G., Welch W. J., Schlossman D. M., Palter K. B., Schlesinger M. J., Rothman J. E. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. Cell 1986; 45: 3–13
   PubMed Web of Science ®Google Scholar
• Chen M. S., Obar R. A., Schroeder C. C., Austin T. W., Poodry C. A., Wadsworth S. C., Vallee R. B. Multiple forms of dynamin are encoded by shibire, a Drosophila gene involved in endocytosis. Nature 1991; 351: 583–586
   PubMed Web of Science ®Google Scholar
• Chen W.-J., Goldstein J. L., Brown M. S. NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor. J. Biol. Chem. 1990; 265: 3116–3123
   PubMed Web of Science ®Google Scholar
• Chestnut M. H., Black M. M., Keen J. H. Axonal transport of clathrin assembly polypeptides (Abstract). J. Cell Biol. 1986; 103: 54a
   Google Scholar
• Collawn J. F., Stangel M., Kuhn L. A., Esekogwu V., Jing S., Trowbridge I. S., Tainer J. A. Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell 1990; 63: 1061–1072
   PubMed Web of Science ®Google Scholar
• Creutz C. E., Harrison J. R. Clathrin light chains and secretory vesicle binding proteins are distinct. Nature 1984; 308: 208–210
   Google Scholar
• De Camilli P., Jahn R. Pathways to regulated exocytosis in neurons. Annu. Rev. Physiol. 1990; 52: 625–645
   PubMed Web of Science ®Google Scholar
• De Waegh S., Brady S. T. Axonal transport of a clathrin uncoating ATPase (HSC70): a role for HSC70 in the modulation of coated vesicle assembly in vivo. J. Neurosci. Res. 1989; 23: 433–440
   Google Scholar
• De Luca-Flaherty C., Mc Kay D. B., Parham P., Hill B. L. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 1990; 62: 875–887
   Google Scholar
• Dodge G. R., Kovalszky I., Mc Bride O. W., Yi H. F., Chu M., Saitta B., Stokes D. G., Iozzo R. V. Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter. Genomics 1991; 11: 174–178
   PubMed Web of Science ®Google Scholar
• Duden R., Griffiths G., Frank R., Argos P., Kreis T. E. β-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to β-adaptin. Cell 1991; 64: 649–665
   PubMed Web of Science ®Google Scholar
• Flynn G. C., Chappell T. G., Rothman J. E. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 1989; 245: 385–390
   PubMed Web of Science ®Google Scholar
• Garner J. A., Lasek R. J. Clathrin is axonally transported as part of slow component b: the microfilament complex. J. Cell Biol. 1981; 88: 172–178
   PubMed Web of Science ®Google Scholar
• Glickman J. N., Conibear E., Pearse B. M. F. Specificity of binding of clathrin adaptors to signals on the mannose-6-phosphate/insulin-like growth factor II receptor. EMBO J. 1989; 8: 1041–1047
   PubMedGoogle Scholar
• Goldstein J. L., Brown M. S., Anderson R. G. W., Russell D. W., Schneider W. J. Receptor-mediated endocytosis: concepts emerging from the LDL receptor system. Annu. Rev. Cell Biol. 1985; 1: 1–39
   PubMedGoogle Scholar
• Gower D. J., Tytell M. Axonal transport of clathrin-associated proteins. Brain Res. 1987; 407: 1–8
   PubMed Web of Science ®Google Scholar
• Greene L. A., Tischler A. S. Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 1976; 73: 2424–2428
   PubMed Web of Science ®Google Scholar
• Greene L. E., Eisenberg E. Dissociation of clathrin from coated vesicles by the uncoating ATPase. J. Biol. Chem. 1990; 265: 6682–6687
   Google Scholar
• Griffiths G., Hoflack B., Simons K., Mellman I., Kornfeld S. The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell 1988; 52: 329–341
   PubMed Web of Science ®Google Scholar
• Heuser J., Kirchhausen T. Deep-etch views of clathrin assemblies. J. Ultrastruct. Res. 1985; 92: 1–27
   Google Scholar
• Heuser J. The role of coated vesicles in the recycling of synaptic vesicle membrane. Cell Biol. Int. Rep. 1989; 13: 1063–1076
   PubMedGoogle Scholar
• Heuser J., Steer C. J. Trimeric binding of the 70-kD uncoating ATPase to the vertices of clathrin triskelia: a candidate intermediate in the vesicle uncoating reaction. J. Cell Biol. 1989; 109: 1457–1466
   Google Scholar
• Heuser J. E., Keen J. Deep-etch visualization of proteins involved in clathrin assembly. J. Cell Biol. 1988; 107: 877–886
   Google Scholar
• Hill B. L., Drickamer K., Brodsky F. M., Parham P. Identification of the phosphorylation sites of clathrin light chain LCb. J. Biol. Chem. 1988; 263: 5499–5501
   Google Scholar
• Holmes N., Biermann J. S., Brodsky F. M., Bharucha D., Parham P. Comparison of the primary structures of clathrin light chains from bovine brain and adrenal gland by peptide mapping. EMBO J. 1984; 3: 1621–1627
   Google Scholar
• Huang X. H., Bomsel M., de Paillerets C., Weintraub H., Alfsen A. Biochemical characterization of algal coated vesicles. Biochimie 1990; 72: 41–49
   Google Scholar
• Huttner W. B., Tooze S. A. Biosynthetic protein transport in the secretory pathway. Curr. Opinion Cell Biol. 1989; 1: 648–654
   Google Scholar
• Jackson A. P., Parham P. Structure of human clathrin light chains. J. Biol. Chem. 1988; 263: 16688–16695
   Google Scholar
• Jackson A. P., Seow H.-F., Holmes N., Drickamer K., Parham P. Clathrin light chains contain brainspecific insertion sequences and a region of homology with intermediate filaments. Nature 1987; 326: 154–159
   Google Scholar
• Keen J. H. Clathrin assembly proteins: affinity purification and a model for coat assembly. J. Cell Biol. 1987; 105: 1989–1998
   Google Scholar
• Keen J. H. Clathrin and associated assembly and disassembly proteins. Annu. Rev. Biochem. 1990; 59: 415–438
   PubMed Web of Science ®Google Scholar
• Keen J. H., Beck K. A. Identification of the clathrinbinding domain of assembly protein AP-2. Biochem. Biophys. Res. Commun. 1989; 158: 17–23
   Google Scholar
• Keen J. H., Beck K. A., Kirchhausen T., Jarrett T. Clathrin domains involved in recognition by assembly protein AP-2. J. Biol. Chem. 1991; 266: 7950–7956
   Google Scholar
• Keen J. H., Black M. M. The phosphorylation of coated membrane proteins in intact neurons. J. Cell Biol. 1986; 102: 1325–1333
   PubMedGoogle Scholar
• Keen J. H., Chestnut M. H., Beck K. A. The clathrin coat assembly polypeptide complex. J. Biol. Chem. 1987; 262: 33864–33871
   Google Scholar
• Keen J. H., Willingham M. C., Pastan I. Clathrincoated vesicles: isolation, dissociation and factor-dependent reassociation of clathrin baskets. Cell 1979; 16: 303–312
   Google Scholar
• Kelly R. B. Secretory granule and synaptic vesicle formation. Curr. Opinion Cell Biol 1991; 3: 654–660
   PubMedGoogle Scholar
• Kelly W. G., Passaniti A., Woods J. W., Daiss J. L., Roth T. F. Tubulin as a molecular component of coated vesicles. J. Cell Biol. 1983; 97: 1191–1199
   Google Scholar
• Kirchhausen T. Identification of a putative yeast homolog of the mammalian β chains of the clathrin-associated protein complexes. Mol. Cell. Biol. 1990; 10: 6089–6090
   PubMedGoogle Scholar
• Kirchhausen T., Davis A. C., Frucht S., O'Brine Greco B., Payne G. S., Tubb B. AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast. J. Biol. Chem. 1991; 266: 11153–11157
   PubMed Web of Science ®Google Scholar
• Kirchhausen T., Harrison S. C. Protein organization in clathrin trimers. Cell 1981; 23: 755–761
   Google Scholar
• Kirchhausen T., Harrison S. C. Structural domains of clathrin heavy chains. J. Cell Biol. 1984; 99: 1725–1734
   Google Scholar
• Kirchhausen T., Harrison S. C., Heuser J. Configuration of clathrin trimers: evidence from electron microscopy. J. Ultrastruct. Mol. Struct. Res. 1986; 94: 199–208
   Google Scholar
• Kirchhausen T., Harrison S. C., Parham P., Brodsky F. M. Location and distribution of the light chains in clathrin trimers. Proc. Natl. Acad. Sci. U.S.A. 1983; 80: 2481–2485
   Google Scholar
• Kirchhausen T., Harrison S. C., Ping Chow E., Mattaliano R. J., Ramachandran K. L., Smart J., Brosius J. Clathrin heavy chain: molecular cloning and complete primary structure. Proc. Natl Acad. Sci. U.S.A. 1987a; 84: 8805–8809
   Google Scholar
• Kirchhausen T., Nathanson K. L., Matsui W., Vaisberg A., Chow E. P., Burne C., Keen J. H., Davis A. E. Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin-associated protein complex AP-2. Proc. Natl. Acad. Sci. U.S.A. 1989; 86: 2612–2616
   PubMedGoogle Scholar
• Kirchhausen T., Scarmato P., Harrison S. C., Monroe J. J., Chow E. P., Mattaliano R. J., Ramachandran K. L., Smart J. E., Ahn A. H., Brosius J. Clathrin light chains LCA and LCB are similar, polymorphic, and share repeated heptad motifs. Science 1987b; 236: 320–324
   Google Scholar
• Klausner R. D., Donaldson J. G., Lippincott-Schwartz J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 1992; 116: 1071–1080
   PubMed Web of Science ®Google Scholar
• Kohtz D. S., Puszkin S. A neuronal protein (NP185) associated with clathrin-coated vesicles. Characterization of NP185 with monoclonal antibodies. J. Biol. Chem. 1988; 263: 7418–7425
   Google Scholar
• Kohtz D. S., Puszkin S. Phosphorylation of tubulin by casein kinase II regulates its binding to a neuronal protein (NP185) associated with brain coated vesicles. J. Neurochem. 1989; 52: 285–295
   Google Scholar
• Kosaka T., Ikeda K. Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibire. J. Cell Biol. 1983; 97: 499–507
   PubMed Web of Science ®Google Scholar
• Ktistakis N. T., Thomas D., Roth M. G. Characteristics of the tyrosine recognition signal for internalization of transmembrane surface glycoproteins. J. Cell Biol? 1990; 111: 1393–1407
   PubMedGoogle Scholar
• Kuenzel E. A., Mulligan J. A., Sommercorn J., Krebs E. G. Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides. J. Biol. Chem. 1987; 262: 9136–9140
   PubMed Web of Science ®Google Scholar
• Lemansky P., Hasilik A., von Figura K., Helmy S., Fishman J., Fine R. E., Kedersha N. L., Rome L. H. Lysosomal enzyme precursors in coated vesicles derived from the exocytic and endocytic pathways. J. Cell Biol. 1987; 104: 1743–1748
   Google Scholar
• Lemmon S. K., Pellicena-Palle A., Conley K., Freund C. L. Sequence of the clathrin heavy chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function. J. Cell Biol. 1991; 112: 65–80
   PubMedGoogle Scholar
• Lenhard J. M., Kahn R. A., Stahl P. D. Evidence for ADP-ribosylation factor (ARF) as a regulator of in vitro endosome-endosome fusion. J. Biol. Chem. 1992; 267: 13047–13052
   PubMedGoogle Scholar
• Leyte A., Barr F. A., Kehlenbach R. H., Huttner W. B. Multiple trimeric G-proteins on the trans-Golgi network exert stimulatory and inhibitory effects on secretory vesicle formation. EMBO J. 1992; 11: 4795–4804
   Google Scholar
• Lin H. B., Harley S., Beevers L. Identification and characterization of plant clathrin light chains. J. Cell Biol. 1991; 115: 187a
   Google Scholar
• Linden C. D., Dedman J. R., Chafouleas J. G., Means A. R., Roth T. F. Interactions of calmodulin with coated vesicles from brain. Proc. Natl. Acad. Sci. U.S.A. 1981; 78: 308–312
   Google Scholar
• Lindner R., Ungewickell E. Clathrin-associated proteins of bovine brain coated vesicles. J. Biol. Chem. 1992; 267: 16567–16573
   PubMedGoogle Scholar
• Lisanti M. P., Schook W., Moskowitz N., Beckenstein K., Bloom W. S., Ores C., Puszkin S. Brain clathrin: studies of its ultrastructural assemblies. Eur. J. Biochem. 1982; 121: 617–622
   PubMedGoogle Scholar
• Lisanti M. P., Shapiro L. S., Moskowitz N., Hua E. L., Puszkin S., Schook W. Isolation and preliminary characterization of clathrin-associated proteins. Eur. J. Biochem. 1982; 125: 463–470
   PubMedGoogle Scholar
• Mahaffey D. T., Moore S. M., Brodsky F. M., Anderson R. G. W. Coat proteins isolated from clathrin coated vesicles can assemble into coated pits. J. Cell Biol. 1989; 108: 1615–1624
   Google Scholar
• Mahaffey D. T., Peeler J. S., Brodsky F. M., Anderson R. G. W. Clathrin-coated pits contain an integral membrane protein that binds the AP-2 subunit with high affinity. J. Biol. Chem. 1990; 265: 16514–16520
   Google Scholar
• Manfredi J. J., Bazari W. L. Purification and characterization of two distinct complexes of assembly polypeptides from calf brain coated vesicles that differ in their polypeptide composition and kinase activities. J. Biol. Chem. 1987; 262: 12182–12188
   Google Scholar
• Matsui W., Kirchhausen T. Stabilization of clathrin coats by the core of the clathrin-associated protein complex AP-2. Biochemistry 1990; 29: 10791–10798
   Google Scholar
• Maycox P. R., Link E., Reetz A., Morris S. A., Jahn R. Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling. J. Cell Biol. 1992; 118: 1379–1388
   Google Scholar
• Mc Intosh D., Timar J., Davies A. J. S. The intracellular movement and cycling of ricin. Eur. J. Cell Biol. 1990; 52: 77–36
   Google Scholar
• Miller S. G., Moore H.-P. Regulated secretion. Curr. Opinion Cell Biol. 1990; 2: 642–647
   Google Scholar
• Mooibroek M. J., Michiel D. F., Wang J. H. Clathrin light chains are calcium-binding proteins. J. Biol. Chem. 1987; 262: 25–28
   Google Scholar
• Moore S. M., Mahaffey D. T., Brodsky F. M., Anderson R. G. W. Assembly of clathrin-coated pits onto purified plasma membranes. Science 1987; 236: 558–563
   Google Scholar
• Morris S. A., Mann A., Ungewickell E. Analysis of 100–180-kDa phosphoproteins in clathrin-coated vesicles from bovine brain. J. Biol. Chem. 1990; 265: 3354–3357
   Google Scholar
• Morris S. A., Schröder S., Plessmann U., Weber K., Ungewickell E. Clathrin assembly protein AP180: primary structure, domain organization and identification of a clathrin binding site. EMBO J. 1993; 12: 667–675
   Google Scholar
• Murphy J.-E., Keen J. H. Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia. J. Biol. Chem. 1992; 267: 10850–10855
   Google Scholar
• Murphy J.-E., Pleasure I. T., Puszkin S., Prasad K., Keen J. H. Clathrin assembly protein AP-3. The identity of the 155K protein, AP180, and NP185 and demonstration of a clathrin binding domain. J. Biol. Chem. 1991; 266: 4401–4408
   Google Scholar
• Nakayama Y., Goebl M., O'Brine Greco B., Lemmon S., Pingchang Chow E., Kirchhausen T. The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast. Eur. J. Biochem. 1991; 202: 569–574
   Google Scholar
• Näthke I., Hill B. L., Parham P., Brodsky F. M. The calcium-binding site of clathrin light chains. J. Biol. Chem. 1990; 265: 18621–18627
   Google Scholar
• Näthke I. S., Heuser J., Lupas A., Stock J., Turck C. W., Brodsky F. M. Folding and trimerization of clathrin subunits at the triskelion hub. Cell 1992; 68: 899–910
   Google Scholar
• O'Halloran T. J., Anderson R. G. W. Characterization of the clathrin heavy chain from Dictyostelium discoideum. DNA Cell Biol. 1992a; 11: 321–330
   Google Scholar
• O'Halloran T. J., Anderson R. G. W. Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium. J. Cell Biol. 1992b; 118: 1371–1377
   Google Scholar
• Orci L., Ravazzola M., Storch M.-J., Anderson R. G. W., Vassalli J.-D., Perrelet A. Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles. Cell 1987; 49: 865–868
   PubMed Web of Science ®Google Scholar
• Parham P., Brodsky F. M., Drickamer K. The occurrence of disulphide bonds in purified clathrin light chains. Biochem. J. 1989; 257: 775–781
   Google Scholar
• Parton R. G., Simons K., Dotti C. G. Axonal and dendritic endocytic pathways in cultured neurons. J. Cell Biol. 1992; 119: 123–137
   PubMed Web of Science ®Google Scholar
• Patzer E. J., Schlossman D. M., Rothman J. E. Release of clathrin from coated vesicles dependent upon a nucleoside triphosphate and a cytosol fraction. J. Cell Biol. 1982; 93: 230–236
   Google Scholar
• Payne G. S. Genetic analysis of clathrin function in yeast. J. Membr. Biol. 1990; 116: 93–105
   PubMedGoogle Scholar
• Payne G. S., Schekman R. A test of clathrin function in protein secretion and cell growth. Science 1985; 230: 1009–1014
   PubMedGoogle Scholar
• Pearse B. M. F. On the structural and functional components of coated vesicles. J. Mol. Biol. 1978; 126: 803–812
   Google Scholar
• Pearse B. M. F. Receptors compete for adaptors found in plasma membrane coated pits. EMBO J. 1988; 7: 3331–3336
   PubMedGoogle Scholar
• Pearse B. M. F., Robinson M. S. Purification and properties of 100-kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 1984; 3: 1951–1957
   Google Scholar
• Pearse B. M. F., Robinson M. S. Clathrin, adaptors, and sorting. Annu. Rev. Cell Biol. 1990; 6: 151–171
   PubMedGoogle Scholar
• Peeler J. S., Donzell W. C., Anderson R. G. W. The appendage domain of the AP-2 subunit is not required for assembly or invagination of clathrin-coated pits. J. Cell Biol. 1993; 120: 47–54
   PubMedGoogle Scholar
• Pfeffer S. R., Drubin D. G., Kelly R. B. Identification of three coated vesicle components as α- and β-tubulin linked to a phosphorylated 50,000-dalton polypeptide. J. Cell Biol. 1983; 97: 40–47
   PubMedGoogle Scholar
• Pley U. M., Hill B. L., Parham P. Localization of the calmodulin binding site in mammalian clathrin light chains LCa and LCb and Ca-requirement for calmodulin binding. J. Cell Biol. 1991; 115: 187a, Abstr.
   Google Scholar
• Ponnambalam S., Robinson M. S., Jackson A. P., Peiperl L., Parham P. Conversation and diversity in families of coated vesicle adaptins. J. Biol. Chem. 1990; 265: 4814–4820
   PubMedGoogle Scholar
• Prasad K., Lippoldt R. E. Molecular characterization of the AP180 coated vesicle assembly protein. Biochemistry 1988; 27: 6098–6104
   Google Scholar
• Robinson M. S. 100-kD coated vesicle proteins: molecular heterogeneity and intracellular distribution studied with monoclonal antibodies. J. Cell Biol. 1987; 104: 887–895
   PubMedGoogle Scholar
• Robinson M. S. Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (α-adaptins). J. Cell Biol. 1989; 108: 833–842
   PubMedGoogle Scholar
• Robinson M. S. Cloning and expression of γ-adaptin, a component of clathrin-coated vesicles associated with the Golgi apparatus. J. Cell Biol. 1990; 111: 2319–2326
   Google Scholar
• Robinson M. S., Kreis T. E. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell 1992; 69: 129–138
   PubMedGoogle Scholar
• Robinson M. S., Pearse B. M. F. Immunofluorescent localization of 100K coated vesicle proteins. J. Cell Biol. 1986; 102: 48–54
   Google Scholar
• Roth T. F., Porter K. R. Yolk protein uptake in the oocyte of the mosquito Aedes aegypti L. J. Cell Biol. 1964; 20: 313–332
   PubMed Web of Science ®Google Scholar
• Rothman J. E., Orci L. Molecular dissection of the secretory pathway. Nature 1992; 355: 409–415
   PubMed Web of Science ®Google Scholar
• Rothman J. E., Schmid S. L. Enzymatic recycling of clathrin from coated vesicles. Cell 1986; 46: 5–9
   PubMedGoogle Scholar
• Scarmato P., Kirchhausen T. Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. J. Biol. Chem. 1990; 265: 3661–3668
   Google Scholar
• Schlossman D. M., Schmid S. L., Braell W. A., Rothman J. E. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 1984; 99: 723–733
   PubMed Web of Science ®Google Scholar
• Schmauss C., Brines M. L., Lerner M. R. The gene encoding the small nuclear ribonucleoprotein-associated protein N is expressed at high levels in neurons. J. Biol. Chem. 1992; 267: 8521–8529
   Google Scholar
• Schmid S. L. The mechanism of receptor-mediated endocytosis: more questions than answers. BioEssays 1992; 14: 589–596
   PubMed Web of Science ®Google Scholar
• Schmid S. L., Braell W. A., Schlossman D. M., Rothman J. E. A role for clathrin light chains in the recognition of clathrin cages by “uncoating ATPase”. Nature 1984; 311: 228–231
   Google Scholar
• Schmid S. L., Matsumoto A. K., Rothman J. E. A domain of clathrin that forms coats. Proc. Natl. Acad. Sci. U.S.A. 1982; 79: 91–95
   Google Scholar
• Schmid S. L., Rothman J. E. Enzymatic dissociation of clathrin cages in a two-stage process. J. Biol. Chem. 1985a; 260: 10044–10049
   PubMedGoogle Scholar
• Schmid S. L., Rothman J. E. Two classes of binding sites for uncoating protein in clathrin triskelions. J. Biol. Chem. 1985b; 260: 10050–10056
   Google Scholar
• Schmid S. L., Smythe E. Stage-specific assays for coated pit formation and coated vesicle budding in vitro. J. Cell Biol. 1991; 114: 869–880
   Google Scholar
• Schook W. J., Puszkin S. Brain clathrin light chain 2 can be phosphorylated by a coated vesicle kinase. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 8039–8043
   Google Scholar
• Schröder S., Ungewickell E. Subunit interaction and function of clathrin-coated vesicle adaptors from the Golgi and the plasma membrane. J. Biol. Chem. 1991; 266: 7910–7918
   Google Scholar
• Seeger M., Payne G. S. Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae. J. Cell Biol. 1992; 118: 531–540
   PubMedGoogle Scholar
• Shapiro S. Z., Webster P. Coated vesicles from the protozoan parasite Trypanosoma brucei: purification and characterization. J. Protozool. 1989; 36: 344–349
   Google Scholar
• Silveira L. A., Wong D. H., Masiarz F. R., Schekman R. Yeast clathrin has a distinctive light chain that is important for cell growth. J. Cell. Biol. 1990; 111: 1437–1449
   PubMedGoogle Scholar
• Smythe E., Carter L. L., Schmid S. L. Cytosol-and clathrin-dependent stimulation of endocytosis in vitro by purified adaptors. J. Cell Biol. 1992; 119: 1163–1171
   Google Scholar
• Smythe E., Pypaert M., Lucocq J., Warren G. Formation of coated vesicles from coated pits in broken A431 cells. J. Cell Biol. 1989; 108: 843–853
   Google Scholar
• Stamm S., Casper D., Dinsmore J., Kaufmann C. A., Brosius J., Helfman D. M. Clathrin light chain B: gene structure and neuron-specific splicing. Nucleic Acids Res. 1992; 20: 5097–5103
   Google Scholar
• Stone G. C., Hammerschlag R. H., Bobinski J. A. Involvement of coated vesicles in the initiation of fast axonal transport. Brain Research 1984; 291: 219–228
   Google Scholar
• Sztul E. S., Melancon P., Howell K. E. Targeting and fusion in vesicular transport. Trends Cell Biol. 1992; 2: 381–386
   Google Scholar
• Thurieau C., Brosius J., Burne C., Jolles P., Keen J. H., Mattaliano R. J., Chow E. P., Ramachandran K. L., Kirchhausen T. Molecular cloning and complete amino acid sequence of AP50, an assembly protein associated with clathrin-coated vesicles. DNA 1988; 7: 663–669
   Google Scholar
• Tooze J., Tooze S. A. Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH- containing secretory granules in AtT20 cells. J. Cell Biol. 1986; 103: 839–850
   PubMed Web of Science ®Google Scholar
• Tooze S. A. Biogenesis of secretory granules. Implications arising from the immature secretory granule in the regulated pathway of secretion. FEBS Lett. 1991; 285: 220–224
   Google Scholar
• Tooze S. A., Huttner W. B. Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell 1990a; 60: 837–847
   Google Scholar
• Tooze S. A., Weiss U., Huttner W. B. Requirement for GTP hydrolysis in the formation of secretory vesicles. Nature 1990b; 347: 207–208
   Google Scholar
• Tytell M., Black M. M., Garner J. A., Lasek R. J. Axonal transport: each major rate component reflects the movement of distinct macromolecular complexes. Science 1981; 214: 179–181
   PubMed Web of Science ®Google Scholar
• Ungewickell E. Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. EMBO J. 1983; 2: 1401–1408
   Google Scholar
• Ungewickell E. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J. 1985; 4: 3385–3391
   PubMed Web of Science ®Google Scholar
• Ungewickell E., Branton D. Assembly units of clathrin coats. Nature 1981; 289: 420–422
   Google Scholar
• Ungewickell E., Ungewickell H. Bovine brain clathrin light chains impede heavy chain assembly in vitro. J. Biol. Chem. 1991; 266: 12710–12714
   Google Scholar
• van der Bliek A. M., Meyerowitz E. M. Dynaminlike protein encoded by the Drosophila shibire gene associated with vesicular traffic. Nature 1991; 351: 411–414
   PubMed Web of Science ®Google Scholar
• Vaux D. The structure of an endocytosis signal. Trends Cell Biol 1992; 2: 189–192
   PubMedGoogle Scholar
• Vigers G. P. A., Crowther R. A., Pearse B. M. F. Location of the the 100 kd-50 kd accessory proteins in clathrin coats. EMBO J. 1986a; 5: 2079–2085
   Google Scholar
• Vigers G. P. A., Crowther R. A., Pearse B. M. F. Three-dimensional structure of clathrin cages in ice. EMBO J. 1986b; 5: 529–534
   Google Scholar
• Virshup D. M., Bennett V. Clathrin-coated vesicle assembly polypeptides: physical properties and reconstitution studies with brain membranes. J. Cell Biol. 1988; 106: 39–50
   PubMedGoogle Scholar
• Webster P. Endocytosis by African trypanosomes. I. Three-dimensional structure of the endocytic organelles in Trypanosoma brucei and T. congolense. Eur. J. Cell Biol 1989; 49: 295–302
   Google Scholar
• Winkler F. K., Stanley K. K. Clathrin heavy chain, light chain interactions. EMBO J. 1983; 2: 1393–1400
   Google Scholar
• Wong D. H., Brodsky F. M. 100-kD Proteins of Golgi- and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties. J. Cell Biol. 1992; 117: 1171–1179
   Google Scholar
• Wong D. H., Ignatius M. J., Parosky G., Parham P., Trojanowski J. Q., Brodsky F. M. Neuron-specific expression of high-molecular-weight clathrin light chain. J. Neurosci. 1990; 10: 3025–3031
   Google Scholar
• Zaremba S., Keen J. H. Assembly polypeptides from coated vesicles mediate reassembly of unique clathrin coats. J. Cell Biol. 1983; 97: 1339–1347
   PubMedGoogle Scholar
• Zaremba S., Keen J. H. Limited proteolytic digestion of coated vesicle assembly polypeptides abolishes reassembly activity. J. Cell. Biochem. 1985; 28: 47–58
   Google Scholar