메뉴 건너뛰기




Volumn 4, Issue C, 1996, Pages 1-32

Receptor-mediated endocytosis

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0001853333     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(96)80003-1     Document Type: Review
Times cited : (3)

References (187)
  • 1
    • 0025077286 scopus 로고
    • Predominance of clathrin light-chain LCb correlates with the presence of a regulated secretory pathway
    • Acton S.L., and Brodsky F.M. Predominance of clathrin light-chain LCb correlates with the presence of a regulated secretory pathway. J. Cell Biol. 111 (1990) 1419-1426
    • (1990) J. Cell Biol. , vol.111 , pp. 1419-1426
    • Acton, S.L.1    Brodsky, F.M.2
  • 2
    • 0027168284 scopus 로고
    • Alteration of clathrin light-chain expression by transfection and gene disruption
    • Acton S.L., Wong D., Parham P., Brodsky F.M., and Jackson A.P. Alteration of clathrin light-chain expression by transfection and gene disruption. Mol. Biol. Cell 4 (1993) 647-660
    • (1993) Mol. Biol. Cell , vol.4 , pp. 647-660
    • Acton, S.L.1    Wong, D.2    Parham, P.3    Brodsky, F.M.4    Jackson, A.P.5
  • 3
    • 0023020763 scopus 로고
    • Purification and properties of a new clathrin assembly protein
    • Ahle S., and Ungewickell E. Purification and properties of a new clathrin assembly protein. EMBO J. 5 (1986) 3143-3149
    • (1986) EMBO J. , vol.5 , pp. 3143-3149
    • Ahle, S.1    Ungewickell, E.2
  • 4
    • 0024317024 scopus 로고
    • Identification of a clathrin binding subunit in the HA2 adaptor protein complex
    • Ahle S., and Ungewickell E. Identification of a clathrin binding subunit in the HA2 adaptor protein complex. J. Biol. Chem. 264 (1989) 20089-20093
    • (1989) J. Biol. Chem. , vol.264 , pp. 20089-20093
    • Ahle, S.1    Ungewickell, E.2
  • 5
    • 0025367497 scopus 로고
    • Auxilin, a newly identified clathrin-associated protein in coated vesicles from bovine brain
    • Ahle S., and Ungewickell E. Auxilin, a newly identified clathrin-associated protein in coated vesicles from bovine brain. J. Cell Biol. 111 (1990) 19-29
    • (1990) J. Cell Biol. , vol.111 , pp. 19-29
    • Ahle, S.1    Ungewickell, E.2
  • 6
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and plasma membrane
    • Ahle S., Mann A., Eichelsbacher H., and Ungewickell E. Structural relationships between clathrin assembly proteins from the Golgi and plasma membrane. EMBO J. 7 (1988) 919-929
    • (1988) EMBO J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, H.3    Ungewickell, E.4
  • 7
    • 0027299702 scopus 로고
    • Dissecting clathrin-coated pits
    • Anderson R.G.W. Dissecting clathrin-coated pits. Trends Cell Biol. 3 (1993) 177-179
    • (1993) Trends Cell Biol. , vol.3 , pp. 177-179
    • Anderson, R.G.W.1
  • 8
    • 0017334127 scopus 로고
    • Role of the coated endocytotic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts
    • Anderson R.G.W., Brown M.S., and Goldstein J.L. Role of the coated endocytotic vesicle in the uptake of receptor-bound low density lipoprotein in human fibroblasts. Cell 10 (1977) 351-364
    • (1977) Cell , vol.10 , pp. 351-364
    • Anderson, R.G.W.1    Brown, M.S.2    Goldstein, J.L.3
  • 9
    • 0026569052 scopus 로고
    • Serotonin-mediated endocytosis of apCAM: An early step of learning-related synaptic growth in Aplysia
    • Bailey C.H., Chen M., Keller F., and Kendel E.R. Serotonin-mediated endocytosis of apCAM: An early step of learning-related synaptic growth in Aplysia. Science 256 (1992) 645-649
    • (1992) Science , vol.256 , pp. 645-649
    • Bailey, C.H.1    Chen, M.2    Keller, F.3    Kendel, E.R.4
  • 10
    • 0026315047 scopus 로고
    • The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation
    • Bansal A., and Gierasch L.M. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell 67 (1991) 1195-1201
    • (1991) Cell , vol.67 , pp. 1195-1201
    • Bansal, A.1    Gierasch, L.M.2
  • 11
    • 0027257424 scopus 로고
    • The Drosophila clathrin heavy-chain gene-clathrin function is essential in a multicellular organism
    • Bazinet C., Katzen A.L., Morgen M., Mahowald A.P., and Lemmon S.K. The Drosophila clathrin heavy-chain gene-clathrin function is essential in a multicellular organism. Genetics 134 (1993) 1119-1134
    • (1993) Genetics , vol.134 , pp. 1119-1134
    • Bazinet, C.1    Katzen, A.L.2    Morgen, M.3    Mahowald, A.P.4    Lemmon, S.K.5
  • 12
    • 15844361829 scopus 로고    scopus 로고
    • The ear of α-adaptin interacts with the COOH-terminal domain of the Eps15 protein
    • Benmerah A., Bègue B., Dautry-Varsat A., and Cerf-Bensussan N. The ear of α-adaptin interacts with the COOH-terminal domain of the Eps15 protein. J. Biol. Chem. 271 (1996) 12111-12116
    • (1996) J. Biol. Chem. , vol.271 , pp. 12111-12116
    • Benmerah, A.1    Bègue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 13
    • 0026516831 scopus 로고
    • Synaptic vesicle membrane-proteins interact to form a multimeric complex
    • Bennett M.K., Calakos N., Kreiner T., and Sheller R.H. Synaptic vesicle membrane-proteins interact to form a multimeric complex. J. Cell Biol. 116 (1992) 761-775
    • (1992) J. Cell Biol. , vol.116 , pp. 761-775
    • Bennett, M.K.1    Calakos, N.2    Kreiner, T.3    Sheller, R.H.4
  • 14
    • 0029989287 scopus 로고    scopus 로고
    • Plant clathrin heavy chain: Sequence analysis and restricted localisation in growing pollen tubes
    • Blackbourn H.D., and Jackson A.P. Plant clathrin heavy chain: Sequence analysis and restricted localisation in growing pollen tubes. J. Cell Sci. 109 (1996) 777-787
    • (1996) J. Cell Sci. , vol.109 , pp. 777-787
    • Blackbourn, H.D.1    Jackson, A.P.2
  • 15
    • 0026080521 scopus 로고
    • Receptor-G protein signalling in yeast
    • Blumer K.J., and Thorner J. Receptor-G protein signalling in yeast. Ann. Rev. Physiol. 53 (1991) 37-57
    • (1991) Ann. Rev. Physiol. , vol.53 , pp. 37-57
    • Blumer, K.J.1    Thorner, J.2
  • 16
    • 0029379646 scopus 로고
    • Role of the regulatory domain of the EGF-receptor cytoplasmic tail in selective binding of the clathrin-associated complex AP2
    • Boll W., Gallusser A., and Kirchhausen T. Role of the regulatory domain of the EGF-receptor cytoplasmic tail in selective binding of the clathrin-associated complex AP2. Curr. Biol. 5 (1995) 1168-1170
    • (1995) Curr. Biol. , vol.5 , pp. 1168-1170
    • Boll, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 18
    • 0024232861 scopus 로고
    • Living with clathrin: Its role in intracellular membrane traffic
    • Brodsky F.M. Living with clathrin: Its role in intracellular membrane traffic. Science 242 (1988) 1396-1402
    • (1988) Science , vol.242 , pp. 1396-1402
    • Brodsky, F.M.1
  • 19
    • 0026519231 scopus 로고
    • Antigen processing and presentation: Close encounters in the endocytic pathway
    • Brodsky F.M. Antigen processing and presentation: Close encounters in the endocytic pathway. Trends Cell Biol. 2 (1992) 109-115
    • (1992) Trends Cell Biol. , vol.2 , pp. 109-115
    • Brodsky, F.M.1
  • 20
    • 0023140616 scopus 로고
    • Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity
    • Brodsky F.M., Galloway C.J., Blank G., Jackson A.P., Seow H.F., Drickamer K., and Parham P. Localization of clathrin light-chain sequences mediating heavy-chain binding and coated vesicle diversity. Nature 326 (1987) 203-205
    • (1987) Nature , vol.326 , pp. 203-205
    • Brodsky, F.M.1    Galloway, C.J.2    Blank, G.3    Jackson, A.P.4    Seow, H.F.5    Drickamer, K.6    Parham, P.7
  • 21
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci C., Parton R.G., Mather L.H., Stannenburg H., Simons K., Hoflack B., and Zerial M. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70 (1992) 715-728
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, L.H.3    Stannenburg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 22
    • 0027498027 scopus 로고
    • Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis
    • Carter L.L., Redelmeier T.E., Woollenweber L.A., and Schmid S.L. Multiple GTP-binding proteins participate in clathrin-coated vesicle-mediated endocytosis. J. Cell Biol. 120 (1993) 37-45
    • (1993) J. Cell Biol. , vol.120 , pp. 37-45
    • Carter, L.L.1    Redelmeier, T.E.2    Woollenweber, L.A.3    Schmid, S.L.4
  • 23
    • 0026344988 scopus 로고
    • Ligand-induced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor
    • Chang C.P., Kao J.P.H., Lazar C.S., Walsh B.J., Wells A., Wiley H.S., Gill G.N., and Rosenfeld M.G. Ligand-induced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor. J. Biol. Chem. 266 (1992) 23467-23470
    • (1992) J. Biol. Chem. , vol.266 , pp. 23467-23470
    • Chang, C.P.1    Kao, J.P.H.2    Lazar, C.S.3    Walsh, B.J.4    Wells, A.5    Wiley, H.S.6    Gill, G.N.7    Rosenfeld, M.G.8
  • 25
    • 0027207340 scopus 로고
    • Adaptor self-aggregation, adaptor-receptor recognition and binding of α-adaptin subunits to the plasma membrane contribute to recruitment of adapter (AP2) components of clathrin-coated pits
    • Chang M.P., Mallet W.G., Mostov K.E., and Brodsky F.M. Adaptor self-aggregation, adaptor-receptor recognition and binding of α-adaptin subunits to the plasma membrane contribute to recruitment of adapter (AP2) components of clathrin-coated pits. EMBO J. 12 (1993) 2169-2180
    • (1993) EMBO J. , vol.12 , pp. 2169-2180
    • Chang, M.P.1    Mallet, W.G.2    Mostov, K.E.3    Brodsky, F.M.4
  • 27
    • 0022534114 scopus 로고
    • Two yeast mutants defective in endocytosis are defective in pheromone response
    • Chvatchko Y., Howald I., and Reizman H. Two yeast mutants defective in endocytosis are defective in pheromone response. Cell 46 (1986) 355-364
    • (1986) Cell , vol.46 , pp. 355-364
    • Chvatchko, Y.1    Howald, I.2    Reizman, H.3
  • 29
    • 0002170988 scopus 로고
    • Structure and molecular organization of higher plant coated vesicles
    • Coleman J., Evans D., Hawes C., Horsley D., and Cole L. Structure and molecular organization of higher plant coated vesicles. J. Cell. Sci. 88 (1987) 35-45
    • (1987) J. Cell. Sci. , vol.88 , pp. 35-45
    • Coleman, J.1    Evans, D.2    Hawes, C.3    Horsley, D.4    Cole, L.5
  • 30
    • 84981667419 scopus 로고
    • Pinocytosis in plants
    • Cram W.J. Pinocytosis in plants. New Phytol. 84 (1980) 1-17
    • (1980) New Phytol. , vol.84 , pp. 1-17
    • Cram, W.J.1
  • 31
    • 0019813567 scopus 로고
    • Assembly and packing of clathrin into coats
    • Crowther R.A., and Pearse B.M.F. Assembly and packing of clathrin into coats. J. Cell Biol. 91 (1981) 790-797
    • (1981) J. Cell Biol. , vol.91 , pp. 790-797
    • Crowther, R.A.1    Pearse, B.M.F.2
  • 32
    • 0025309605 scopus 로고
    • Pathway to regulated endocytosis in neurones
    • DeCamilli P., and Jahn R. Pathway to regulated endocytosis in neurones. Ann. Rev. Physiol. 52 (1990) 625-645
    • (1990) Ann. Rev. Physiol. , vol.52 , pp. 625-645
    • DeCamilli, P.1    Jahn, R.2
  • 33
    • 0025126351 scopus 로고
    • Uncoating protein Hsc70 binds a conformationally labile domain of clathrin light-chain LCa to stimulate ATP hydrolysis
    • DeLuca-Flaherty C., McKay D.B., Parham P., and Hill B.L. Uncoating protein Hsc70 binds a conformationally labile domain of clathrin light-chain LCa to stimulate ATP hydrolysis. Cell 62 (1990) 875-887
    • (1990) Cell , vol.62 , pp. 875-887
    • DeLuca-Flaherty, C.1    McKay, D.B.2    Parham, P.3    Hill, B.L.4
  • 34
    • 0344583446 scopus 로고
    • Improved coated vesicle isolation allows better characterization of clathrin polypeptides
    • Demmer A., Holstein S.E.H., Hinz G., Schauermann G., and Robinson D.G. Improved coated vesicle isolation allows better characterization of clathrin polypeptides. J. Exp. Bot. 44 (1993) 23-33
    • (1993) J. Exp. Bot. , vol.44 , pp. 23-33
    • Demmer, A.1    Holstein, S.E.H.2    Hinz, G.3    Schauermann, G.4    Robinson, D.G.5
  • 35
    • 0007391753 scopus 로고
    • The isolation and enrichment of coated vesicles from suspension cultured carrot cells
    • Depta H., and Robinson D.G. The isolation and enrichment of coated vesicles from suspension cultured carrot cells. Protoplasma 130 (1986) 162-170
    • (1986) Protoplasma , vol.130 , pp. 162-170
    • Depta, H.1    Robinson, D.G.2
  • 36
    • 0028128334 scopus 로고
    • ARF: a key regulatory switch in membrane traffic and organelle structure
    • Donaldson J.G., and Klausner R.D. ARF: a key regulatory switch in membrane traffic and organelle structure. Cur. Op. in Cell Biol. 6 (1994) 527-532
    • (1994) Cur. Op. in Cell Biol. , vol.6 , pp. 527-532
    • Donaldson, J.G.1    Klausner, R.D.2
  • 37
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting lysosome
    • Dunn K.W., McGraw T.E., and Maxfield F.R. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting lysosome. J. Cell Biol. 109 (1989) 3303-3314
    • (1989) J. Cell Biol. , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 39
    • 0025359062 scopus 로고
    • Kinase-activity controls the sorting of the epidermal growth-factor receptor within the multivesicular body
    • Felder S., Miller K., Moehren G., Ullrich A., Schlessinger J., and Hopkins C.R. Kinase-activity controls the sorting of the epidermal growth-factor receptor within the multivesicular body. Cell 61 (1990) 623-634
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1    Miller, K.2    Moehren, G.3    Ullrich, A.4    Schlessinger, J.5    Hopkins, C.R.6
  • 40
    • 0001888685 scopus 로고
    • Ultrastructural cytology of the endocytotic pathway in plants
    • Endocytosis, Exocytosis and Vesicle Traffic in Plants. Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds), Cambridge University Press
    • Fowke L.C., Tanchak M.A., and Galway M.E. Ultrastructural cytology of the endocytotic pathway in plants. In: Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds). Endocytosis, Exocytosis and Vesicle Traffic in Plants. Society for Experimental Biology, 45 (1991), Cambridge University Press 15-40
    • (1991) Society for Experimental Biology, 45 , pp. 15-40
    • Fowke, L.C.1    Tanchak, M.A.2    Galway, M.E.3
  • 41
    • 0027396215 scopus 로고
    • Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth-factor receptor
    • Futter C.E., Felder J., Schlessinger J., Ullrich A., and Hopkins C.R. Annexin I is phosphorylated in the multivesicular body during the processing of the epidermal growth-factor receptor. J. Cell Biol. 120 (1993) 77-83
    • (1993) J. Cell Biol. , vol.120 , pp. 77-83
    • Futter, C.E.1    Felder, J.2    Schlessinger, J.3    Ullrich, A.4    Hopkins, C.R.5
  • 42
    • 0020028428 scopus 로고
    • Immunocytochemical localization of the receptor for asialoglycoprotein in rat liver
    • Geuze H.J., Slot W., Strous G.J.A.M., Lodish H.F., and Schwartz A.L. Immunocytochemical localization of the receptor for asialoglycoprotein in rat liver. J. Cell Biol. 92 (1982) 865-870
    • (1982) J. Cell Biol. , vol.92 , pp. 865-870
    • Geuze, H.J.1    Slot, W.2    Strous, G.J.A.M.3    Lodish, H.F.4    Schwartz, A.L.5
  • 44
    • 0026201202 scopus 로고
    • Small GTP-binding proteins and their role in transport
    • Goud B., and McCaffrey M. Small GTP-binding proteins and their role in transport. Cur. Op. Cell Biol. 3 (1991) 626-633
    • (1991) Cur. Op. Cell Biol. , vol.3 , pp. 626-633
    • Goud, B.1    McCaffrey, M.2
  • 45
    • 0021947313 scopus 로고
    • Assembled and unassembled pools of clathrin: A quantitative study using an enzyme immunoassay
    • Goud B., Huet C., and Louvard D. Assembled and unassembled pools of clathrin: A quantitative study using an enzyme immunoassay. J. Cell Biol. 100 (1985) 521-527
    • (1985) J. Cell Biol. , vol.100 , pp. 521-527
    • Goud, B.1    Huet, C.2    Louvard, D.3
  • 46
    • 0025231301 scopus 로고
    • Dissociation of clathrin from coated vesicles by uncoating ATPase
    • Greene L.E., and Eisenberg E. Dissociation of clathrin from coated vesicles by uncoating ATPase. J. Biol. Chem. 265 (1990) 6682-6687
    • (1990) J. Biol. Chem. , vol.265 , pp. 6682-6687
    • Greene, L.E.1    Eisenberg, E.2
  • 47
    • 0024449827 scopus 로고
    • Membrane traffic in endocytosis: Insights from cell-free assays
    • Gruenberg J., and Howell K.E. Membrane traffic in endocytosis: Insights from cell-free assays. Ann. Rev. Cell Biol. 5 (1989) 453-482
    • (1989) Ann. Rev. Cell Biol. , vol.5 , pp. 453-482
    • Gruenberg, J.1    Howell, K.E.2
  • 48
    • 0025817708 scopus 로고
    • The argument for pre-existing early and late endosomes
    • Griffiths G., and Gruenberg J. The argument for pre-existing early and late endosomes. Trends Cell Biol. 1 (1991) 59
    • (1991) Trends Cell Biol. , vol.1 , pp. 59
    • Griffiths, G.1    Gruenberg, J.2
  • 49
    • 0025014816 scopus 로고
    • Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment
    • Guagliardi L.E., Koppelman B., Blum J.S., Marks M.S., Creswell P., and Brodsky F.M. Co-localization of molecules involved in antigen processing and presentation in an early endocytic compartment. Nature 343 (1990) 133-139
    • (1990) Nature , vol.343 , pp. 133-139
    • Guagliardi, L.E.1    Koppelman, B.2    Blum, J.S.3    Marks, M.S.4    Creswell, P.5    Brodsky, F.M.6
  • 50
    • 2842546967 scopus 로고
    • Isolation and partial characterization of clathrin-coated vesicles from pea (Pisum sativum L.) cotyledons
    • Harley S.M., and Beevers L. Isolation and partial characterization of clathrin-coated vesicles from pea (Pisum sativum L.) cotyledons. Protoplasma 150 (1989) 103-109
    • (1989) Protoplasma , vol.150 , pp. 103-109
    • Harley, S.M.1    Beevers, L.2
  • 51
    • 0020574786 scopus 로고
    • Clathrin, cages and coated vesicles
    • Harrison S.C., and Kirchhausen T. Clathrin, cages and coated vesicles. Cell 33 (1983) 650-652
    • (1983) Cell , vol.33 , pp. 650-652
    • Harrison, S.C.1    Kirchhausen, T.2
  • 52
    • 0029935911 scopus 로고    scopus 로고
    • In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting
    • Heilker R., Manning-Krieg, Zuber J.F., and Spiess M. In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J. 15 (1996) 2893-2899
    • (1996) EMBO J. , vol.15 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg2    Zuber, J.F.3    Spiess, M.4
  • 53
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • Heuser J.E. Three-dimensional visualization of coated vesicle formation in fibroblasts. J. Cell Biol. 84 (1980) 560-583
    • (1980) J. Cell Biol. , vol.84 , pp. 560-583
    • Heuser, J.E.1
  • 54
    • 0024501531 scopus 로고
    • Effects of cytoplasmic acidification on clathrin lattice morphology
    • Heuser J.E. Effects of cytoplasmic acidification on clathrin lattice morphology. J. Cell Biol. 108 (1989) 401-411
    • (1989) J. Cell Biol. , vol.108 , pp. 401-411
    • Heuser, J.E.1
  • 55
    • 0024816522 scopus 로고
    • The role of coated vesicles in the recycling of synaptic vesicle membrane
    • Heuser J.E. The role of coated vesicles in the recycling of synaptic vesicle membrane. Cell Biol. Intl. Rep. 13 (1989) 1063-1076
    • (1989) Cell Biol. Intl. Rep. , vol.13 , pp. 1063-1076
    • Heuser, J.E.1
  • 56
    • 0024075871 scopus 로고
    • Deep-etch visualization of proteins involved in clathrin assembly
    • Heuser J.E., and Keen J. Deep-etch visualization of proteins involved in clathrin assembly. J. Cell Biol. 107 (1988) 877-886
    • (1988) J. Cell Biol. , vol.107 , pp. 877-886
    • Heuser, J.E.1    Keen, J.2
  • 57
    • 0024433249 scopus 로고
    • Trimeric binding of the 70KD uncoating ATPase to the vertices of clathrin triskelia: A candidate intermediate in the vesicle uncoating reaction
    • Heuser J.E., and Steer C.J. Trimeric binding of the 70KD uncoating ATPase to the vertices of clathrin triskelia: A candidate intermediate in the vesicle uncoating reaction. J. Cell Biol. 109 (1989) 1457-1466
    • (1989) J. Cell Biol. , vol.109 , pp. 1457-1466
    • Heuser, J.E.1    Steer, C.J.2
  • 58
    • 0023945674 scopus 로고
    • Identification of the phosphorylation sites of clathrin light chain LCb
    • Hill B.L., Drickamer K., Brodsky F.M., and Parham P. Identification of the phosphorylation sites of clathrin light chain LCb. J. Biol. Chem. 263 (1988) 5499-5501
    • (1988) J. Biol. Chem. , vol.263 , pp. 5499-5501
    • Hill, B.L.1    Drickamer, K.2    Brodsky, F.M.3    Parham, P.4
  • 59
    • 0013639228 scopus 로고
    • Confirmation of endocytosis in higher plant protoplasts using lectin-gold conjugates
    • Hillmer S., Depta H., and Robinson D.G. Confirmation of endocytosis in higher plant protoplasts using lectin-gold conjugates. Eur. J. Cell Biol. 41 (1986) 142-149
    • (1986) Eur. J. Cell Biol. , vol.41 , pp. 142-149
    • Hillmer, S.1    Depta, H.2    Robinson, D.G.3
  • 60
    • 1142263560 scopus 로고
    • Uptake of lucifer yellow CH in leaves of Commelina communis is mediated by endocytosis
    • Hillmer S., Hedrich R., Robert-Nicoud M., and Robinson D.G. Uptake of lucifer yellow CH in leaves of Commelina communis is mediated by endocytosis. Protoplasma 158 (1990) 142-148
    • (1990) Protoplasma , vol.158 , pp. 142-148
    • Hillmer, S.1    Hedrich, R.2    Robert-Nicoud, M.3    Robinson, D.G.4
  • 61
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J.E., and Schmid S.L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 374 (1995) 190-192
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 62
    • 0027157601 scopus 로고
    • The prominent 28kDa polypeptide in clathrin coated vesicle fractions from developing pea cotyledons is contaminating ferritin
    • Hoh B., and Robinson D.G. The prominent 28kDa polypeptide in clathrin coated vesicle fractions from developing pea cotyledons is contaminating ferritin. Cell Biol. Intl. 17 (1993) 551-557
    • (1993) Cell Biol. Intl. , vol.17 , pp. 551-557
    • Hoh, B.1    Robinson, D.G.2
  • 63
    • 0028178629 scopus 로고
    • Identification of a β-type adaptin in plant clathrin-coated vesicles
    • Holstein S.E.H., Drucker M., and Robinson D.G. Identification of a β-type adaptin in plant clathrin-coated vesicles. J. Cell Sci. 107 (1994) 945-953
    • (1994) J. Cell Sci. , vol.107 , pp. 945-953
    • Holstein, S.E.H.1    Drucker, M.2    Robinson, D.G.3
  • 64
    • 0020601856 scopus 로고
    • Internalization and processing of transferrin and transferrin receptor in human carcinoma A431 cells
    • Hopkins C.R., and Trowbridge I.S. Internalization and processing of transferrin and transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97 (1983) 508-521
    • (1983) J. Cell Biol. , vol.97 , pp. 508-521
    • Hopkins, C.R.1    Trowbridge, I.S.2
  • 65
    • 0025281993 scopus 로고
    • Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum
    • Hopkins C.R., Gibson A., Shipman M., and Miller K. Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum. Nature 346 (1990) 335-339
    • (1990) Nature , vol.346 , pp. 335-339
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Miller, K.4
  • 66
    • 0000989463 scopus 로고
    • Receptor-mediated endocytosis in plant cells
    • Horn M.A., Heinstein P.F., and Low P.S. Receptor-mediated endocytosis in plant cells. Plant Cell 1 (1989) 1003-1009
    • (1989) Plant Cell , vol.1 , pp. 1003-1009
    • Horn, M.A.1    Heinstein, P.F.2    Low, P.S.3
  • 67
    • 0005907748 scopus 로고
    • Biotin-mediated delivery of exogenous macromolecules into soybean cells
    • Horn M.A., Heinstein P.F., and Low P.S. Biotin-mediated delivery of exogenous macromolecules into soybean cells. Plant Physiol. 93 (1990) 1492-1496
    • (1990) Plant Physiol. , vol.93 , pp. 1492-1496
    • Horn, M.A.1    Heinstein, P.F.2    Low, P.S.3
  • 68
    • 0001672151 scopus 로고
    • Characterization of parameters influencing receptor-mediated endocytosis in cultured soybean cells
    • Horn M.A., Heinstein P.F., and Low P.S. Characterization of parameters influencing receptor-mediated endocytosis in cultured soybean cells. Plant Physiol. 98 (1992) 673-679
    • (1992) Plant Physiol. , vol.98 , pp. 673-679
    • Horn, M.A.1    Heinstein, P.F.2    Low, P.S.3
  • 69
    • 0027233570 scopus 로고
    • 5-HT and cAMP induce the formation of coated pits and vesicles and increase the expression of clathrin light-chain in sensory neurons of Aplysia
    • Hu Y.H., Barzilai A., Chen M., Bailey C.H., and Kendel E.R. 5-HT and cAMP induce the formation of coated pits and vesicles and increase the expression of clathrin light-chain in sensory neurons of Aplysia. Neuron 10 (1993) 921-929
    • (1993) Neuron , vol.10 , pp. 921-929
    • Hu, Y.H.1    Barzilai, A.2    Chen, M.3    Bailey, C.H.4    Kendel, E.R.5
  • 70
    • 0023127462 scopus 로고
    • Clathrin light-chains contain brain-specific insertion sequences and a region of homology with intermediate filaments
    • Jackson A.P., Seow H.-F., Holmes N.J., Drickmer K., and Parham P. Clathrin light-chains contain brain-specific insertion sequences and a region of homology with intermediate filaments. Nature 326 (1987) 154-159
    • (1987) Nature , vol.326 , pp. 154-159
    • Jackson, A.P.1    Seow, H.-F.2    Holmes, N.J.3    Drickmer, K.4    Parham, P.5
  • 71
    • 0023734573 scopus 로고
    • Structure of human clathrin light-chains
    • Jackson A.P., and Parham P. Structure of human clathrin light-chains. J. Biol. Chem. 263 (1988) 16688-16695
    • (1988) J. Biol. Chem. , vol.263 , pp. 16688-16695
    • Jackson, A.P.1    Parham, P.2
  • 72
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone in S. cerevisiae
    • Jenness D.D., and Spatrick P. Down regulation of the α-factor pheromone in S. cerevisiae. Cell 46 (1986) 345-353
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 73
    • 0021433359 scopus 로고
    • Endocytosis of cationic ferritin by bean leaf protoplasts
    • Joachim S., and Robinson D.G. Endocytosis of cationic ferritin by bean leaf protoplasts. Eur. J. Cell Biol. 34 (1984) 212-216
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 212-216
    • Joachim, S.1    Robinson, D.G.2
  • 74
    • 0014541501 scopus 로고
    • The vesicle in a basket
    • Kanaseki T., and Kadota K. The vesicle in a basket. J. Cell Biol. 42 (1969) 202-219
    • (1969) J. Cell Biol. , vol.42 , pp. 202-219
    • Kanaseki, T.1    Kadota, K.2
  • 75
    • 0025345414 scopus 로고
    • Clathrin and associated assembly and disassembly proteins
    • Keen J.H. Clathrin and associated assembly and disassembly proteins. Ann. Rev. Biochem. 59 (1990) 415-438
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 415-438
    • Keen, J.H.1
  • 76
    • 0022549471 scopus 로고
    • The phosphorylation of coated membrane proteins in intact neurons
    • Keen J.H., and Black M.M. The phosphorylation of coated membrane proteins in intact neurons. J. Cell. Biol. 102 (1986) 1325-1333
    • (1986) J. Cell. Biol. , vol.102 , pp. 1325-1333
    • Keen, J.H.1    Black, M.M.2
  • 77
    • 0025776846 scopus 로고
    • Clathrin domains involved in recognition by assembly protein AP2
    • Keen J.H., Beck K.A., Kirchhausen T., and Jarrett T. Clathrin domains involved in recognition by assembly protein AP2. J. Biol. Chem. 166 (1991) 7950-7956
    • (1991) J. Biol. Chem. , vol.166 , pp. 7950-7956
    • Keen, J.H.1    Beck, K.A.2    Kirchhausen, T.3    Jarrett, T.4
  • 78
    • 0018344979 scopus 로고
    • Clathrin-coated vesicles: Isolation, dissociation and factor-dependent reassociation of clathrin baskets
    • Keen J.H., Willingham M.C., and Pastan I.H. Clathrin-coated vesicles: Isolation, dissociation and factor-dependent reassociation of clathrin baskets. Cell 16 (1979) 303-312
    • (1979) Cell , vol.16 , pp. 303-312
    • Keen, J.H.1    Willingham, M.C.2    Pastan, I.H.3
  • 79
    • 0025059483 scopus 로고
    • Identification of a putative yeast homolog of the mammalian β-chains of the clathrin-associated protein complexes
    • Kirchhausen T. Identification of a putative yeast homolog of the mammalian β-chains of the clathrin-associated protein complexes. Mol. Cell. Biol. 10 (1990) 6089-6090
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6089-6090
    • Kirchhausen, T.1
  • 80
    • 0019435922 scopus 로고
    • Protein organisation in clathrin trimers
    • Kirchhausen T.K., and Harrison S.C. Protein organisation in clathrin trimers. Cell 23 (1981) 755-761
    • (1981) Cell , vol.23 , pp. 755-761
    • Kirchhausen, T.K.1    Harrison, S.C.2
  • 81
    • 0027195836 scopus 로고
    • Immunoelectron microscopic evidence for the extended conformation of light-chains in clathrin trimers
    • Kirchhausen T.K., and Toyoda T. Immunoelectron microscopic evidence for the extended conformation of light-chains in clathrin trimers. J. Biol. Chem. 268 (1993) 10268-10273
    • (1993) J. Biol. Chem. , vol.268 , pp. 10268-10273
    • Kirchhausen, T.K.1    Toyoda, T.2
  • 82
    • 0025737052 scopus 로고
    • AP17 and AP19. The mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast
    • Kirchhausen T., Davies A.C., Frucht S., O'Brine Greco B., Payne G.S., and 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. 266 (1991) 11153-11157
    • (1991) J. Biol. Chem. , vol.266 , pp. 11153-11157
    • Kirchhausen, T.1    Davies, A.C.2    Frucht, S.3    O'Brine Greco, B.4    Payne, G.S.5    Tubb, B.6
  • 88
    • 0024296831 scopus 로고
    • A neuronal protein (NP185) associated with clathrin-coated vesicles. Characterization of NP185 with monoclonal antibodies
    • Kohtz D.S., and Puszkin S. A neuronal protein (NP185) associated with clathrin-coated vesicles. Characterization of NP185 with monoclonal antibodies. J. Biol. Chem. 263 (1988) 7418-7425
    • (1988) J. Biol. Chem. , vol.263 , pp. 7418-7425
    • Kohtz, D.S.1    Puszkin, S.2
  • 89
    • 0020807636 scopus 로고
    • Reversible blockage of membrane retrieval and endocytosis in the Garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibire
    • Kosaka T., and 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. 97 (1983) 499-507
    • (1983) J. Cell Biol. , vol.97 , pp. 499-507
    • Kosaka, T.1    Ikeda, K.2
  • 90
    • 0020603664 scopus 로고
    • Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila
    • Kosaka T., and Ikeda K. Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila. J. Neurobiol. 14 (1983) 207-225
    • (1983) J. Neurobiol. , vol.14 , pp. 207-225
    • Kosaka, T.1    Ikeda, K.2
  • 91
    • 0027260748 scopus 로고
    • Actin and fimbrin are required for the internalization step of endocytosis in yeast
    • Kubler E., and Riezman H. Actin and fimbrin are required for the internalization step of endocytosis in yeast. EMBO J. 12 (1993) 2855-2862
    • (1993) EMBO J. , vol.12 , pp. 2855-2862
    • Kubler, E.1    Riezman, H.2
  • 92
    • 0024276904 scopus 로고
    • A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits
    • Lazarovits J., and Roth M. A single amino acid change in the cytoplasmic domain allows the influenza virus hemagglutinin to be endocytosed through coated pits. Cell 53 (1988) 743-752
    • (1988) Cell , vol.53 , pp. 743-752
    • Lazarovits, J.1    Roth, M.2
  • 93
    • 0023663065 scopus 로고
    • Clathrin requirement for normal growth of yeast
    • Lemmon S.K., and Jones E.W. Clathrin requirement for normal growth of yeast. Science 238 (1987) 504-509
    • (1987) Science , vol.238 , pp. 504-509
    • Lemmon, S.K.1    Jones, E.W.2
  • 94
    • 0026007817 scopus 로고
    • Sequence of the clathrin heavy-chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function
    • Lemmon S.K., Pellicena-Palle A., Conley K., and Freund C.L. Sequence of the clathrin heavy-chain from Saccharomyces cerevisiae and requirement of the COOH terminus for clathrin function. J. Cell Biol. 112 (1991) 65-80
    • (1991) J. Cell Biol. , vol.112 , pp. 65-80
    • Lemmon, S.K.1    Pellicena-Palle, A.2    Conley, K.3    Freund, C.L.4
  • 95
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains
    • Letourneur F., and Klausner R.D. A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 69 (1992) 1143-1157
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 96
    • 0027055310 scopus 로고
    • Multiplicity of clathrin light-chain-like polypeptides from developing pea (Pisum sativum L.) cotyledons
    • Lin H.-B., Harley S.M., Butler J.M., and Beevers L. Multiplicity of clathrin light-chain-like polypeptides from developing pea (Pisum sativum L.) cotyledons. J. Cell Sci. 103 (1992) 1127-1137
    • (1992) J. Cell Sci. , vol.103 , pp. 1127-1137
    • Lin, H.-B.1    Harley, S.M.2    Butler, J.M.3    Beevers, L.4
  • 97
    • 0028858382 scopus 로고
    • Regulation of clathrin assembly and trimerisation defined using recombinant triskelion hubs
    • Lin S.H., Wong M.L., Craik C.S., and Brodsky F.M. Regulation of clathrin assembly and trimerisation defined using recombinant triskelion hubs. Cell 83 (1995) 257-267
    • (1995) Cell , vol.83 , pp. 257-267
    • Lin, S.H.1    Wong, M.L.2    Craik, C.S.3    Brodsky, F.M.4
  • 99
    • 0026709661 scopus 로고
    • Clathrin-associated proteins of bovine brain coated vesicles
    • Lindner R., and Ungewickell E. Clathrin-associated proteins of bovine brain coated vesicles. J. Biol. Chem. 267 (1992) 16567-16573
    • (1992) J. Biol. Chem. , vol.267 , pp. 16567-16573
    • Lindner, R.1    Ungewickell, E.2
  • 100
    • 0000247251 scopus 로고
    • Comparison of elicitor and vitamin receptor-mediated endocytosis in cultured soybean cells
    • Low P.S., Legendre L., Heinstein P.F., and Horn M.A. Comparison of elicitor and vitamin receptor-mediated endocytosis in cultured soybean cells. J. Exp. Bot. 44 (1993) 269-274
    • (1993) J. Exp. Bot. , vol.44 , pp. 269-274
    • Low, P.S.1    Legendre, L.2    Heinstein, P.F.3    Horn, M.A.4
  • 101
    • 0027514907 scopus 로고
    • Eukaryotic membrane traffic: Retrieval and retention mechanisms to achieve organelle residence
    • Luzio J.P., and Banting G. Eukaryotic membrane traffic: Retrieval and retention mechanisms to achieve organelle residence. Trends Biochem. Sci. 18 (1993) 395-398
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 395-398
    • Luzio, J.P.1    Banting, G.2
  • 102
    • 0024554517 scopus 로고
    • Coat proteins isolated from clathrin coated vesicles can assemble into coated pits
    • Mahaffey D.T., Moore M.S., Brodsky F.M., and Anderson R.G.W. Coat proteins isolated from clathrin coated vesicles can assemble into coated pits. J. Cell Biol. 108 (1989) 1615-1624
    • (1989) J. Cell Biol. , vol.108 , pp. 1615-1624
    • Mahaffey, D.T.1    Moore, M.S.2    Brodsky, F.M.3    Anderson, R.G.W.4
  • 103
    • 0026727853 scopus 로고
    • Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling
    • Maycox P.R., Link E., Reetz A., Morris S.A., and Jahn R. Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling. J. Cell Biol. 118 (1992) 1379-1388
    • (1992) J. Cell Biol. , vol.118 , pp. 1379-1388
    • Maycox, P.R.1    Link, E.2    Reetz, A.3    Morris, S.A.4    Jahn, R.5
  • 104
    • 0027243406 scopus 로고
    • Sorting of membrane-components from endosomes and subsequent recycling to the cell-surface occurs by a bulk flow process
    • Mayor S., Presley J.F., and Maxfield F.R. Sorting of membrane-components from endosomes and subsequent recycling to the cell-surface occurs by a bulk flow process. J. Cell Biol. 121 (1993) 1257-1269
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 105
    • 0024373375 scopus 로고
    • Regulatory role for GTP-binding proteins in endocytosis
    • Mayorga L.S., Diaz R., and Stahl P.D. Regulatory role for GTP-binding proteins in endocytosis. Science 244 (1989) 1475-1477
    • (1989) Science , vol.244 , pp. 1475-1477
    • Mayorga, L.S.1    Diaz, R.2    Stahl, P.D.3
  • 106
    • 2842569283 scopus 로고
    • The isolation of coated vesicles from protoplasts of soybean
    • Mersey B.G., Griffing L.R., Rennie P.J., and Fowke L.C. The isolation of coated vesicles from protoplasts of soybean. Planta 163 (1985) 317-327
    • (1985) Planta , vol.163 , pp. 317-327
    • Mersey, B.G.1    Griffing, L.R.2    Rennie, P.J.3    Fowke, L.C.4
  • 107
    • 0026505543 scopus 로고
    • Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization
    • Miettinen H.M., Matter K., Hunziker W., Rose J.K., and Mellman I. Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization. J. Cell Biol. 116 (1992) 875-888
    • (1992) J. Cell Biol. , vol.116 , pp. 875-888
    • Miettinen, H.M.1    Matter, K.2    Hunziker, W.3    Rose, J.K.4    Mellman, I.5
  • 108
    • 0009204160 scopus 로고
    • Post Golgi apparatus structures and membrane removal in plants
    • Mollenhauer H.H., Morre D.J., and Griffing L.R. Post Golgi apparatus structures and membrane removal in plants. Protoplasma 162 (1991) 55-60
    • (1991) Protoplasma , vol.162 , pp. 55-60
    • Mollenhauer, H.H.1    Morre, D.J.2    Griffing, L.R.3
  • 109
    • 0027511162 scopus 로고
    • Clathrin assembly protein AP180: Primary structure, domain organisation and identification of a clathrin binding site
    • Morris S.A., Schröder S., Plessmann U., Weber K., and Ungewickell E. Clathrin assembly protein AP180: Primary structure, domain organisation and identification of a clathrin binding site. EMBO J. 12 (1993) 667-675
    • (1993) EMBO J. , vol.12 , pp. 667-675
    • Morris, S.A.1    Schröder, S.2    Plessmann, U.3    Weber, K.4    Ungewickell, E.5
  • 110
    • 0021353734 scopus 로고
    • Identification of coated vesicles in Saccharomyces cerevisiae
    • Mueller S.C., and Branton D. Identification of coated vesicles in Saccharomyces cerevisiae. J. Cell Biol. 98 (1984) 341-346
    • (1984) J. Cell Biol. , vol.98 , pp. 341-346
    • Mueller, S.C.1    Branton, D.2
  • 111
    • 0025808286 scopus 로고
    • Maturation models for endosome and lysosome biogenesis
    • Murphy R.F. Maturation models for endosome and lysosome biogenesis. Trends Cell Biol. 1 (1991) 77-82
    • (1991) Trends Cell Biol. , vol.1 , pp. 77-82
    • Murphy, R.F.1
  • 113
    • 0025084547 scopus 로고
    • The clacium-binding site of clathrin light chains
    • Näthke I., Hill B.L., Parham P., and Brodsky F.M. The clacium-binding site of clathrin light chains. J. Biol. Chem. 265 (1990) 18621-18627
    • (1990) J. Biol. Chem. , vol.265 , pp. 18621-18627
    • Näthke, I.1    Hill, B.L.2    Parham, P.3    Brodsky, F.M.4
  • 114
    • 0026503136 scopus 로고
    • Folding and trimerization of clathrin subunits at the triskelion hub
    • Näthke I.S., Heuser J., Lupas A., Stock J., Turck C.W., and Brodsky F.M. Folding and trimerization of clathrin subunits at the triskelion hub. Cell 68 (1992) 899-910
    • (1992) Cell , vol.68 , pp. 899-910
    • Näthke, I.S.1    Heuser, J.2    Lupas, A.3    Stock, J.4    Turck, C.W.5    Brodsky, F.M.6
  • 115
    • 0027390598 scopus 로고
    • Suppressors of clathrin deficiency: Overexpression of ubiquitin rescues lethal strains of clathrin deficient Saccharomyces cerivisiae
    • Nelson K.K., and Lemmon S.K. Suppressors of clathrin deficiency: Overexpression of ubiquitin rescues lethal strains of clathrin deficient Saccharomyces cerivisiae. Mol. Cell. Biol. 13 (1993) 521-532
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 521-532
    • Nelson, K.K.1    Lemmon, S.K.2
  • 116
    • 0000642690 scopus 로고
    • Hydrolysis of protein in vacuoles isolated from higher plant tissue
    • Nishimura M., and Beevers H. Hydrolysis of protein in vacuoles isolated from higher plant tissue. Nature 277 (1979) 412-413
    • (1979) Nature , vol.277 , pp. 412-413
    • Nishimura, M.1    Beevers, H.2
  • 117
    • 0025835882 scopus 로고
    • Lucifer Yellow and fluorescein isothiocyanate uptake by cells of Morinda citrifolia in suspension cultures is not confined to the endocytic pathway
    • O'Driscoll D., Wilson G., and Steer M.W. Lucifer Yellow and fluorescein isothiocyanate uptake by cells of Morinda citrifolia in suspension cultures is not confined to the endocytic pathway. J. Cell Sci. 100 (1991) 237-241
    • (1991) J. Cell Sci. , vol.100 , pp. 237-241
    • O'Driscoll, D.1    Wilson, G.2    Steer, M.W.3
  • 118
    • 0026756246 scopus 로고
    • Characterization of the clathrin heavy chain from Dictytostelium discoideum
    • O'Halloran T.J., and Anderson R.G.W. Characterization of the clathrin heavy chain from Dictytostelium discoideum. DNA and Cell Biol. 11 (1992) 321-330
    • (1992) DNA and Cell Biol. , vol.11 , pp. 321-330
    • O'Halloran, T.J.1    Anderson, R.G.W.2
  • 119
    • 0026671869 scopus 로고
    • Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles and development in Dictyostelium
    • O'Halloran T.J., and Anderson R.G.W. Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles and development in Dictyostelium. J. Cell Biol. 118 (1992) 1371-1377
    • (1992) J. Cell Biol. , vol.118 , pp. 1371-1377
    • O'Halloran, T.J.1    Anderson, R.G.W.2
  • 121
    • 0028838515 scopus 로고
    • Targeting signals and subunit interactions in coated vesicle adaptor complexes
    • Page L.J., and Robinson M.S. Targeting signals and subunit interactions in coated vesicle adaptor complexes. J. Cell Biol. 131 (1995) 619-630
    • (1995) J. Cell Biol. , vol.131 , pp. 619-630
    • Page, L.J.1    Robinson, M.S.2
  • 122
    • 0022344231 scopus 로고
    • A test of clathrin function in protein secretion and cell growth
    • Payne G.S., and Schekman R. A test of clathrin function in protein secretion and cell growth. Science 230 (1985) 1009-1014
    • (1985) Science , vol.230 , pp. 1009-1014
    • Payne, G.S.1    Schekman, R.2
  • 123
    • 0023440747 scopus 로고
    • Genetic and biochemical characterization of clathrin-deficient Saccharomyces cerevisiae
    • Payne G.S., Hasson T.B., Hasson M.S., and Schekman R. Genetic and biochemical characterization of clathrin-deficient Saccharomyces cerevisiae. Mol. Cell. Biol. 7 (1987) 3888-3898
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3888-3898
    • Payne, G.S.1    Hasson, T.B.2    Hasson, M.S.3    Schekman, R.4
  • 124
    • 0023891818 scopus 로고
    • Protein transport to the vacuole and receptor mediated endocytosis by clathrin heavy chain-deficient yeast
    • Payne G.S., Baker D., Van Tuinen E., and Schekman R. Protein transport to the vacuole and receptor mediated endocytosis by clathrin heavy chain-deficient yeast. J. Cell Biol. 106 (1988) 1453-1461
    • (1988) J. Cell Biol. , vol.106 , pp. 1453-1461
    • Payne, G.S.1    Baker, D.2    Van Tuinen, E.3    Schekman, R.4
  • 125
    • 0018276996 scopus 로고
    • On the structural and functional components of coated vesicles
    • Pearse B.M.F. On the structural and functional components of coated vesicles. J. Mol. Biol. 126 (1978) 803-812
    • (1978) J. Mol. Biol. , vol.126 , pp. 803-812
    • Pearse, B.M.F.1
  • 126
    • 0023413042 scopus 로고
    • Clathrin and coated vesicles
    • Pearse B.M.F. Clathrin and coated vesicles. EMBO J. 6 (1987) 2507-2512
    • (1987) EMBO J. , vol.6 , pp. 2507-2512
    • Pearse, B.M.F.1
  • 127
    • 0024120843 scopus 로고
    • Receptors compete for adaptors found in plasma membrane coated pits
    • Pearse B.M.F. Receptors compete for adaptors found in plasma membrane coated pits. EMBO J. 7 (1988) 3331-3336
    • (1988) EMBO J. , vol.7 , pp. 3331-3336
    • Pearse, B.M.F.1
  • 128
    • 0021487739 scopus 로고
    • Purification and properties of 100kDa proteins from coated vesicles and their reconstitution with clathrin
    • Pearse B.M.F., and Robinson M.S. Purification and properties of 100kDa proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 3 (1984) 1951-1957
    • (1984) EMBO J. , vol.3 , pp. 1951-1957
    • Pearse, B.M.F.1    Robinson, M.S.2
  • 130
    • 0027505622 scopus 로고
    • The appendage domain of the AP2 subunit is not required for assembly or invagination of clathrin-coated pits
    • Peeler J.S., Donzell W.C., and Anderson R.G.W. The appendage domain of the AP2 subunit is not required for assembly or invagination of clathrin-coated pits. J. Cell. Biol. 120 (1993) 47-54
    • (1993) J. Cell. Biol. , vol.120 , pp. 47-54
    • Peeler, J.S.1    Donzell, W.C.2    Anderson, R.G.W.3
  • 132
    • 0028906643 scopus 로고
    • The interaction of calmodulin with clathrin-coated vesicles, triskelions and light-chains
    • Pley U.M., Hill B.L., Alibert C., Brodsky F.M., and Parham P. The interaction of calmodulin with clathrin-coated vesicles, triskelions and light-chains. J. Biol. Chem. 270 (1995) 2395-2402
    • (1995) J. Biol. Chem. , vol.270 , pp. 2395-2402
    • Pley, U.M.1    Hill, B.L.2    Alibert, C.3    Brodsky, F.M.4    Parham, P.5
  • 134
    • 0023580315 scopus 로고
    • Apparent endocytosis of fluorescein isothiocyanate conjguated dextran by Saccharomyces cerevisiae reflects uptake of low-molecular weight impurities, not dextran
    • Preston R.A., Murphy R.F., and Jones E.W. Apparent endocytosis of fluorescein isothiocyanate conjguated dextran by Saccharomyces cerevisiae reflects uptake of low-molecular weight impurities, not dextran. J. Cell Biol. 105 (1987) 1981-1987
    • (1987) J. Cell Biol. , vol.105 , pp. 1981-1987
    • Preston, R.A.1    Murphy, R.F.2    Jones, E.W.3
  • 136
    • 0026006536 scopus 로고
    • Newly synthesized synaptophysin is transported to synaptic-like microvesicles via constitutive secretory vesicles and the plasma membrane
    • Regnier-Vigouroux A., Tooze S.A., and Huttner W.B. Newly synthesized synaptophysin is transported to synaptic-like microvesicles via constitutive secretory vesicles and the plasma membrane. EMBO J. 10 (1991) 3589-3601
    • (1991) EMBO J. , vol.10 , pp. 3589-3601
    • Regnier-Vigouroux, A.1    Tooze, S.A.2    Huttner, W.B.3
  • 138
    • 84995056622 scopus 로고
    • Vacuolar lucifer yellow uptake in plants: Endocytosis or anion transport; a critical opinion
    • Robinson D.G., and Hedrich R. Vacuolar lucifer yellow uptake in plants: Endocytosis or anion transport; a critical opinion. Botanica Acta 104 (1991) 257-264
    • (1991) Botanica Acta , vol.104 , pp. 257-264
    • Robinson, D.G.1    Hedrich, R.2
  • 139
    • 1842361211 scopus 로고
    • Legumin antibodies recognize polypeptides in coated vesicles isolated from developing pea cotyledons
    • Robinson D.G., Balusek K., and Freundt H. Legumin antibodies recognize polypeptides in coated vesicles isolated from developing pea cotyledons. Protoplasma 150 (1989) 79-82
    • (1989) Protoplasma , vol.150 , pp. 79-82
    • Robinson, D.G.1    Balusek, K.2    Freundt, H.3
  • 140
    • 77956725573 scopus 로고
    • Isolation and characterisation of plant coated vesicles
    • Endocytosis, Exocytosis and Vesicle Traffic in Plants. Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds), Cambridge University Press, Cambridge
    • Robinson D.G., Balusek K., Depta H., Hoh B., and Holstein S.E.H. Isolation and characterisation of plant coated vesicles. In: Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds). Endocytosis, Exocytosis and Vesicle Traffic in Plants. Society for Experimental Biology, 45 (1991), Cambridge University Press, Cambridge 65-79
    • (1991) Society for Experimental Biology, 45 , pp. 65-79
    • Robinson, D.G.1    Balusek, K.2    Depta, H.3    Hoh, B.4    Holstein, S.E.H.5
  • 141
    • 0024523484 scopus 로고
    • Cloning of cDNAs encoding two related 100kD coated vesicle proteins (α-adaptins)
    • Robinson M.S. Cloning of cDNAs encoding two related 100kD coated vesicle proteins (α-adaptins). J. Cell Biol. 108 (1989) 833-842
    • (1989) J. Cell Biol. , vol.108 , pp. 833-842
    • Robinson, M.S.1
  • 142
    • 0025642375 scopus 로고
    • Cloning and expression of γ-adaptin. A component of clathrin-coated vesicles associated with the Golgi apparatus
    • Robinson M.S. Cloning and expression of γ-adaptin. A component of clathrin-coated vesicles associated with the Golgi apparatus. J. Cell Biol. 111 (1990) 2319-2326
    • (1990) J. Cell Biol. , vol.111 , pp. 2319-2326
    • Robinson, M.S.1
  • 143
    • 0027490848 scopus 로고
    • Assembly and targeting of adaptin chimeras in transfected cells
    • Robinson M.S. Assembly and targeting of adaptin chimeras in transfected cells. J. Cell Biol. 123 (1993) 67-77
    • (1993) J. Cell Biol. , vol.123 , pp. 67-77
    • Robinson, M.S.1
  • 144
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of Brefeldin A and G protein activators
    • Robinson M.S., and Kreis T.E. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of Brefeldin A and G protein activators. Cell 69 (1992) 129-138
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 145
    • 0027207946 scopus 로고
    • Identification of a novel sequence mediating regulated endocytosis of the G-protein coupled α-pheremone receptor in yeast
    • Rohrer J., Benedetti H., Zanolari B., and Riezman H. Identification of a novel sequence mediating regulated endocytosis of the G-protein coupled α-pheremone receptor in yeast. Mol. Biol. Cell 4 (1993) 511-521
    • (1993) Mol. Biol. Cell , vol.4 , pp. 511-521
    • Rohrer, J.1    Benedetti, H.2    Zanolari, B.3    Riezman, H.4
  • 146
    • 0023493988 scopus 로고
    • Oligosaccharide signalling in plants
    • Ryan C.A. Oligosaccharide signalling in plants. Ann. Rev. Cell Biol. 3 (1987) 295-317
    • (1987) Ann. Rev. Cell Biol. , vol.3 , pp. 295-317
    • Ryan, C.A.1
  • 147
    • 0005547032 scopus 로고
    • Receptor-mediated endocytosis in plants is energetically possible
    • Saxton M.J., and Breidenbach R.W. Receptor-mediated endocytosis in plants is energetically possible. Plant Physiol. 86 (1988) 993-995
    • (1988) Plant Physiol. , vol.86 , pp. 993-995
    • Saxton, M.J.1    Breidenbach, R.W.2
  • 148
    • 0021206453 scopus 로고
    • A role for clathrin light-chains in the recognition of clathrin cages by uncoating ATPase
    • Schmid S.L., Braell W.A., Schlossman D.M., and Rothman J.E. A role for clathrin light-chains in the recognition of clathrin cages by uncoating ATPase. Nature 311 (1984) 228-231
    • (1984) Nature , vol.311 , pp. 228-231
    • Schmid, S.L.1    Braell, W.A.2    Schlossman, D.M.3    Rothman, J.E.4
  • 149
    • 0026928718 scopus 로고
    • The mechanism of receptor-mediated endocytosis: More questions that answers
    • Schmid S.L. The mechanism of receptor-mediated endocytosis: More questions that answers. Bioessays 14 (1992) 589-596
    • (1992) Bioessays , vol.14 , pp. 589-596
    • Schmid, S.L.1
  • 150
    • 0027406045 scopus 로고
    • Coated-vesicle formation in vitro: Conflicting results using different assays
    • Schmid S.L. Coated-vesicle formation in vitro: Conflicting results using different assays. Trends Cell Biol. 3 (1993) 145-148
    • (1993) Trends Cell Biol. , vol.3 , pp. 145-148
    • Schmid, S.L.1
  • 151
  • 152
    • 0027371110 scopus 로고
    • Targeting of plasma membrane adaptors in vitro
    • Seaman M.N.J., Ball C.J., and Robinson M.S. Targeting of plasma membrane adaptors in vitro. J. Cell Biol. 123 (1993) 1093-1105
    • (1993) J. Cell Biol. , vol.123 , pp. 1093-1105
    • Seaman, M.N.J.1    Ball, C.J.2    Robinson, M.S.3
  • 153
    • 0026742306 scopus 로고
    • Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane-protein retention in Saccharomyces cerevisiae
    • Seeger M., and Payne G.S. Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane-protein retention in Saccharomyces cerevisiae. J. Cell Biol. 118 (1992) 531-540
    • (1992) J. Cell Biol. , vol.118 , pp. 531-540
    • Seeger, M.1    Payne, G.S.2
  • 154
    • 0029584896 scopus 로고
    • A clathrin binding site in the hinge of β2 chain of mammalian AP2 complexes
    • Shih W.G., Gallusser A., and Kirchhausen T. A clathrin binding site in the hinge of β2 chain of mammalian AP2 complexes. J. Biol. Chem. 270 (1995) 31083-31090
    • (1995) J. Biol. Chem. , vol.270 , pp. 31083-31090
    • Shih, W.G.1    Gallusser, A.2    Kirchhausen, T.3
  • 155
    • 0025132351 scopus 로고
    • Yeast clathrin has a distinctive light chain that is important for cell growth
    • Silveira L.A., Wong D.H., Masiarz F.R., and Schekman R. Yeast clathrin has a distinctive light chain that is important for cell growth. J. Cell Biol. 111 (1990) 1437-1449
    • (1990) J. Cell Biol. , vol.111 , pp. 1437-1449
    • Silveira, L.A.1    Wong, D.H.2    Masiarz, F.R.3    Schekman, R.4
  • 156
    • 0024546840 scopus 로고
    • Formation of coated vesicles from coated pits in broken A431 cells
    • Smythe E., Pypaert M., Lucocq J., and Warren G. Formation of coated vesicles from coated pits in broken A431 cells. J. Cell Biol. 108 (1989) 843-853
    • (1989) J. Cell Biol. , vol.108 , pp. 843-853
    • Smythe, E.1    Pypaert, M.2    Lucocq, J.3    Warren, G.4
  • 157
    • 0026446697 scopus 로고
    • Cytosol and clathrin-dependent stimulation of endocytosis in vitro by purified adaptors
    • Smythe E., Carter L.L., and Schmid S. Cytosol and clathrin-dependent stimulation of endocytosis in vitro by purified adaptors. J. Cell Biol. 119 (1992) 1163-1171
    • (1992) J. Cell Biol. , vol.119 , pp. 1163-1171
    • Smythe, E.1    Carter, L.L.2    Schmid, S.3
  • 158
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin A., and Waters G.M. Endocytosis of growth factor receptors. Bioessays 15 (1993) 375-381
    • (1993) Bioessays , vol.15 , pp. 375-381
    • Sorkin, A.1    Waters, G.M.2
  • 159
    • 0027249993 scopus 로고
    • Interaction of activated EGF receptors with coated pit adaptins
    • Sorkin A., and Carpenter G. Interaction of activated EGF receptors with coated pit adaptins. Science 261 (1993) 612-615
    • (1993) Science , vol.261 , pp. 612-615
    • Sorkin, A.1    Carpenter, G.2
  • 160
    • 0001390003 scopus 로고
    • Plasma membrane turnover in plant cells
    • Steer M.W. Plasma membrane turnover in plant cells. J. Exp. Bot. 39 (1988) 987-996
    • (1988) J. Exp. Bot. , vol.39 , pp. 987-996
    • Steer, M.W.1
  • 161
    • 0002547154 scopus 로고
    • Vesicle dynamics and membrane turnover in plant cells
    • Endocytosis, Exocytosis and Vesicle Traffic in Plants. Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds), Cambridge University Press, Cambridge
    • Steer M.W., and O'Driscoll D. Vesicle dynamics and membrane turnover in plant cells. In: Hawes C.R., Coleman J.O.D., and Evans D.E. (Eds). Endocytosis, Exocytosis and Vesicle Traffic in Plants. Society for Experimental Biology, 45 (1991), Cambridge University Press, Cambridge 129-142
    • (1991) Society for Experimental Biology, 45 , pp. 129-142
    • Steer, M.W.1    O'Driscoll, D.2
  • 162
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., and De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTPγS in nerve terminals. Nature 374 (1995) 186-190
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 163
    • 0029894198 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin
    • Takei K., Mundigl O., Daniell L., and DeCamilli P. The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin. J. Cell Biol. 133 (1996) 1237-1250
    • (1996) J. Cell Biol. , vol.133 , pp. 1237-1250
    • Takei, K.1    Mundigl, O.2    Daniell, L.3    DeCamilli, P.4
  • 164
    • 0001628825 scopus 로고
    • Endocytosis of cationized ferritin by coated vesicles of soybean protoplasts
    • Tanchak M.A., Griffing L.R., Mersey B.G., and Fowke L.C. Endocytosis of cationized ferritin by coated vesicles of soybean protoplasts. Planta 162 (1984) 481-486
    • (1984) Planta , vol.162 , pp. 481-486
    • Tanchak, M.A.1    Griffing, L.R.2    Mersey, B.G.3    Fowke, L.C.4
  • 165
    • 0008342761 scopus 로고
    • The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis
    • Tanchak M.A., and Fowke L.C. The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis. Protoplasma 138 (1987) 173-182
    • (1987) Protoplasma , vol.138 , pp. 173-182
    • Tanchak, M.A.1    Fowke, L.C.2
  • 166
    • 0001346114 scopus 로고
    • Ultrastructure of the partially coated reticulum and dictyosomes during endocytosis by soybean protoplasts
    • Tanchak M.A., Rennie P.J., and Fowke L.C. Ultrastructure of the partially coated reticulum and dictyosomes during endocytosis by soybean protoplasts. Planta 175 (1988) 433-441
    • (1988) Planta , vol.175 , pp. 433-441
    • Tanchak, M.A.1    Rennie, P.J.2    Fowke, L.C.3
  • 167
    • 0018581730 scopus 로고
    • 125I-labelled insulin by isolated hepatocytes and H4 hepatoma cells
    • 125I-labelled insulin by isolated hepatocytes and H4 hepatoma cells. Can. J. Biochem. 57 (1979) 459-468
    • (1979) Can. J. Biochem. , vol.57 , pp. 459-468
    • Terris, S.1    Hofman, A.C.2    Steiner, D.F.3
  • 169
    • 0022427782 scopus 로고
    • The 70kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles
    • Ungewickell E. The 70kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J. 4 (1985) 3385-3391
    • (1985) EMBO J. , vol.4 , pp. 3385-3391
    • Ungewickell, E.1
  • 170
    • 0019890534 scopus 로고
    • Assembly units of clathrin coats
    • Ungewickell E., and Branton D. Assembly units of clathrin coats. Nature 289 (1981) 420-422
    • (1981) Nature , vol.289 , pp. 420-422
    • Ungewickell, E.1    Branton, D.2
  • 171
    • 0025900858 scopus 로고
    • Bovine brain clathrin light chains impede heavy chain assembly in vitro
    • Ungewickell E., and Ungewickell H. Bovine brain clathrin light chains impede heavy chain assembly in vitro. J. Biol. Chem. 266 (1991) 12710-12714
    • (1991) J. Biol. Chem. , vol.266 , pp. 12710-12714
    • Ungewickell, E.1    Ungewickell, H.2
  • 173
    • 0025810110 scopus 로고
    • Dynamin-like protein encoded by the Drosophila shibire gene, associated with vesicular traffic
    • van der Bliek A.M., and Meyerowitz E.M. Dynamin-like protein encoded by the Drosophila shibire gene, associated with vesicular traffic. Nature 351 (1991) 411-414
    • (1991) Nature , vol.351 , pp. 411-414
    • van der Bliek, A.M.1    Meyerowitz, E.M.2
  • 175
    • 0026730464 scopus 로고
    • The small GTP-binding protein rab4 controls an early sorting event on the endocytotic pathway
    • van der Sluijs P., Hull M., Webster P., Male P., Gould B., and Mellman I. The small GTP-binding protein rab4 controls an early sorting event on the endocytotic pathway. Cell 70 (1992) 729-740
    • (1992) Cell , vol.70 , pp. 729-740
    • van der Sluijs, P.1    Hull, M.2    Webster, P.3    Male, P.4    Gould, B.5    Mellman, I.6
  • 176
    • 0026735184 scopus 로고
    • The structure of an endocytosis signal
    • Vaux D. The structure of an endocytosis signal. Trends Cell Biol. 2 (1992) 189-192
    • (1992) Trends Cell Biol. , vol.2 , pp. 189-192
    • Vaux, D.1
  • 177
    • 0022684837 scopus 로고
    • Three dimensional structure of clathrin cages in ice
    • Vigers G.P.A., Crowther R.A., and Pearse B.M.F. Three dimensional structure of clathrin cages in ice. EMBO J. 5 (1986) 529-534
    • (1986) EMBO J. , vol.5 , pp. 529-534
    • Vigers, G.P.A.1    Crowther, R.A.2    Pearse, B.M.F.3
  • 178
    • 0242632066 scopus 로고
    • Endocytosis in plant protoplasts: Visualization and quantitation of fluid-phase endocytosis using silver-enhanced bovine serum albumin-gold
    • Villanueva M.A., Taylor J., Sui X., and Griffing L.R. Endocytosis in plant protoplasts: Visualization and quantitation of fluid-phase endocytosis using silver-enhanced bovine serum albumin-gold. J. Exp. Bot. 44 (1993) 275-281
    • (1993) J. Exp. Bot. , vol.44 , pp. 275-281
    • Villanueva, M.A.1    Taylor, J.2    Sui, X.3    Griffing, L.R.4
  • 180
    • 0026786340 scopus 로고
    • Endocytosis: What goes in and how?
    • Watts C., and Marsh M. Endocytosis: What goes in and how?. J. Cell Sci. 103 (1992) 1-8
    • (1992) J. Cell Sci. , vol.103 , pp. 1-8
    • Watts, C.1    Marsh, M.2
  • 181
    • 0021092725 scopus 로고
    • Clathrin heavy-chain light-chain interactions
    • Winkler F.K., and Stanley K.K. Clathrin heavy-chain light-chain interactions. EMBO J. 2 (1983) 1393-1400
    • (1983) EMBO J. , vol.2 , pp. 1393-1400
    • Winkler, F.K.1    Stanley, K.K.2
  • 182
    • 0026628312 scopus 로고
    • 100 kD proteins of golgi and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties
    • Wong D.H., and 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. 117 (1992) 1171-1179
    • (1992) J. Cell Biol. , vol.117 , pp. 1171-1179
    • Wong, D.H.1    Brodsky, F.M.2
  • 184
    • 0026073421 scopus 로고
    • Isolation of functional, coated, endocytic vesicles
    • Woodman P.G., and Warren G. Isolation of functional, coated, endocytic vesicles. J. Cell Biol. 112 (1991) 1133-1141
    • (1991) J. Cell Biol. , vol.112 , pp. 1133-1141
    • Woodman, P.G.1    Warren, G.2
  • 185
    • 0021734410 scopus 로고
    • Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway
    • Yamashiro D.J., Tycko B., Fluss S.R., and Maxfield F.R. Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway. Cell 37 (1984) 789-800
    • (1984) Cell , vol.37 , pp. 789-800
    • Yamashiro, D.J.1    Tycko, B.2    Fluss, S.R.3    Maxfield, F.R.4
  • 186
    • 0026493590 scopus 로고
    • Yeast pheromone receptor endocytosis and hyperphosphorylation are independent of G protein-mediated signal transduction
    • Zanolari B., Raths S., Singer-Kruger B., and Riezman H. Yeast pheromone receptor endocytosis and hyperphosphorylation are independent of G protein-mediated signal transduction. Cell 71 (1992) 755-763
    • (1992) Cell , vol.71 , pp. 755-763
    • Zanolari, B.1    Raths, S.2    Singer-Kruger, B.3    Riezman, H.4
  • 187
    • 0027640399 scopus 로고
    • Rab GTPases in vesicular transport
    • Zerial M., and Stenmark H. Rab GTPases in vesicular transport. Curr. Op. Cell Biol. 5 (1993) 613-620
    • (1993) Curr. Op. Cell Biol. , vol.5 , pp. 613-620
    • Zerial, M.1    Stenmark, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.