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Volumn 160, Issue 5, 2003, Pages 699-708

AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation

Author keywords

Adaptor protein 1; Clathrin coated vesicle; Phosphoregulation; Protein phosphatase 2A; Uncoating

Indexed keywords

ADAPTOR PROTEIN; CELL MEMBRANE PROTEIN; HEAT SHOCK PROTEIN 70; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; UNCLASSIFIED DRUG;

EID: 0037416130     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200211080     Document Type: Article
Times cited : (100)

References (59)
  • 1
    • 0027973055 scopus 로고
    • ATPase activity associated with the uncoating of clathrin baskets by Hsp70
    • Barouch, W., K. Prasad, L.E. Greene, and E. Eisenberg. 1994. ATPase activity associated with the uncoating of clathrin baskets by Hsp70. J. Biol. Chem. 269:28563-28568.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28563-28568
    • Barouch, W.1    Prasad, K.2    Greene, L.E.3    Eisenberg, E.4
  • 2
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid and tautomycin
    • Bertrand, F., P. Turowski, and B.A. Hemmings. 1997. Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid and tautomycin. J. Biol. Chem. 272:13856-13863.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13856-13863
    • Bertrand, F.1    Turowski, P.2    Hemmings, B.A.3
  • 3
    • 0021471706 scopus 로고
    • Dissociation of clathrin coats coupled to the hydrolysis of ATP: Role of an uncoating ATPase
    • Braell, W.A., D.M. Schlossman, S.L. Schmid, and J.E. Rothman. 1984. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J. Cell Biol. 99:734-741.
    • (1984) J. Cell Biol. , vol.99 , pp. 734-741
    • Braell, W.A.1    Schlossman, D.M.2    Schmid, S.L.3    Rothman, J.E.4
  • 4
    • 0032502661 scopus 로고    scopus 로고
    • A region from the medium chain adaptor subunit (μ) recognizes leucine- and tyrosine-based sorting signals
    • Bremnes, T., V. Lauvrak, B. Lindqvist, and O. Bakke. 1998. A region from the medium chain adaptor subunit (μ) recognizes leucine- and tyrosine-based sorting signals. J. Biol. Chem. 273:8638-8645.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8638-8645
    • Bremnes, T.1    Lauvrak, V.2    Lindqvist, B.3    Bakke, O.4
  • 5
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • Collins, B.M., A.J. McCoy, H.M. Kent, P.R. Evans, and D.J. Owen. 2002. Molecular architecture and functional model of the endocytic AP2 complex. Cell. 109:523-535.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 6
    • 0037018152 scopus 로고    scopus 로고
    • Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis
    • Conner, S.D., and S.L. Schmid. 2002. Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J. Cell Biol. 156:921-929.
    • (2002) J. Cell Biol. , vol.156 , pp. 921-929
    • Conner, S.D.1    Schmid, S.L.2
  • 7
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittie, A.S., L. Thomas, G. Thomas, and S.A. Tooze. 1997. Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. EMBO J. 16:4859-4870.
    • (1997) EMBO J. , vol.16 , pp. 4859-4870
    • Dittie, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 8
    • 0035152740 scopus 로고    scopus 로고
    • γ subunit of the AP-1 adaptor complex binds clathrin: Implications for cooperative binding in clathrin vesicle assembly
    • Doray, B., and S. Kornfeld. 2001. γ subunit of the AP-1 adaptor complex binds clathrin: implications for cooperative binding in clathrin vesicle assembly. Mol. Biol. Cell. 12:1925-1935.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1925-1935
    • Doray, B.1    Kornfeld, S.2
  • 9
    • 0037062410 scopus 로고    scopus 로고
    • Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif
    • Doray, B., K. Bruns, P. Ghosh, and S.A. Kornfeld. 2002a. Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif. Proc. Natl. Acad. Sci. USA. 99:8072-8077.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8072-8077
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.A.4
  • 10
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray, B., P. Ghosh, J. Griffith, H. Geuze, and S. Kornfeld. 2002b. Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science. 297:1700-1703.
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.4    Kornfeld, S.5
  • 11
    • 0033739794 scopus 로고    scopus 로고
    • The assembly ofAP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes
    • Drake, M.T., Y. Zhu, and S. Kornfeld. 2000. The assembly ofAP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes. Mol. Biol. Cell. 11:3723-3736.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3723-3736
    • Drake, M.T.1    Zhu, Y.2    Kornfeld, S.3
  • 12
    • 0035937156 scopus 로고    scopus 로고
    • Binding of AP2 to sorting signals is modulated by AP2 phosphorylation
    • Fingerhut, A., K. von Figura, and S. Honing. 2001. Binding of AP2 to sorting signals is modulated by AP2 phosphorylation. J. Biol. Chem. 276:5476-5482.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5476-5482
    • Fingerhut, A.1    Von Figura, K.2    Honing, S.3
  • 13
    • 0031465375 scopus 로고    scopus 로고
    • Platelet adhesion to collagen activates a phosphoprotein complex of heat-shock proteins and protein phosphatase 1
    • Gear, A.R., C.G. Simon, and R. Polanowska-Grabowska. 1997. Platelet adhesion to collagen activates a phosphoprotein complex of heat-shock proteins and protein phosphatase 1. J. Neural Transm. 104:1037-1047.
    • (1997) J. Neural Transm. , vol.104 , pp. 1037-1047
    • Gear, A.R.1    Simon, C.G.2    Polanowska-Grabowska, R.3
  • 14
    • 0033978513 scopus 로고    scopus 로고
    • Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells
    • Greener, T., X. Xhao, H. Nojima, E. Eisenberg, and L.E. Greene. 2000. Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells. J. Biol. Chem. 275:1365-1370.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1365-1370
    • Greener, T.1    Xhao, X.2    Nojima, H.3    Eisenberg, E.4    Greene, L.E.5
  • 15
    • 0031859055 scopus 로고    scopus 로고
    • ATP- and cytosol-dependent release of adaptor proteins from clathrin-coated vesicles: A dual role for Hsc70
    • Hannan, L.A., S.L. Newmyer, and S.L. Schmid. 1998. ATP- and cytosol-dependent release of adaptor proteins from clathrin-coated vesicles: a dual role for Hsc70. Mol. Biol. Cell. 9:2217-2229.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2217-2229
    • Hannan, L.A.1    Newmyer, S.L.2    Schmid, S.L.3
  • 16
    • 0023945674 scopus 로고
    • Identification of the phosphorylation sites of clathrin light chain LCb
    • Hill, B.L., K. Drickamer, F.M. Brodsky, and P. Parham. 1988. Identification of the phosphorylation sites of clathrin light chain LCb. J. Biol. Chem. 263:5499-5501.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5499-5501
    • Hill, B.L.1    Drickamer, K.2    Brodsky, F.M.3    Parham, P.4
  • 17
    • 0039109677 scopus 로고    scopus 로고
    • The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors
    • Honing, S., M. Sosa, A. Hille-Rehfeld, and K. von Figura. 1997. The 46-kDa mannose 6-phosphate receptor contains multiple binding sites for clathrin adaptors. J. Biol. Chem. 272:19884-19890.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19884-19890
    • Honing, S.1    Sosa, M.2    Hille-Rehfeld, A.3    Von Figura, K.4
  • 18
    • 0035021147 scopus 로고    scopus 로고
    • Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells
    • Huang, F., A. Nesterov, R.E. Carter, and A. Sorkin. 2001. Trafficking of yellow-fluorescent-protein-tagged μ1 subunit of clathrin adaptor AP-1 complex in living cells. Traffic. 2:345-357.
    • (2001) Traffic , vol.2 , pp. 345-357
    • Huang, F.1    Nesterov, A.2    Carter, R.E.3    Sorkin, A.4
  • 21
    • 0031023433 scopus 로고    scopus 로고
    • GAK: A cyclin G associated kinase contains a tensin/auxilin-like domain
    • Kanaoka, Y., S.H. Kimura, I. Okazaki, M. Ikeda, and H. Nojima. 1997. GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain. FEBS Lett. 402:73-80.
    • (1997) FEBS Lett. , vol.402 , pp. 73-80
    • Kanaoka, Y.1    Kimura, S.H.2    Okazaki, I.3    Ikeda, M.4    Nojima, H.5
  • 22
    • 0031238793 scopus 로고    scopus 로고
    • Structure, expression, and chromosomal localization of human GAK
    • Kimura, S.H., H. Tsuruga, N. Yabuta, Y. Endo, and H. Nojima. 1997. Structure, expression, and chromosomal localization of human GAK. Genomics. 44:179-187.
    • (1997) Genomics , vol.44 , pp. 179-187
    • Kimura, S.H.1    Tsuruga, H.2    Yabuta, N.3    Endo, Y.4    Nojima, H.5
  • 24
    • 0036300863 scopus 로고    scopus 로고
    • CK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesicles
    • Korolchuk, V.I., and G. Banting. 2002. CK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesicles. Traffic. 3:428-439.
    • (2002) Traffic , vol.3 , pp. 428-439
    • Korolchuk, V.I.1    Banting, G.2
  • 25
    • 0034692508 scopus 로고    scopus 로고
    • β2-adaptin is constitutively de-phosphorylared by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase
    • Lauritsen, J.P., C. Menne, J. Kastrup, J. Dietrich, N. Odum, and C. Geisler. 2000. β2-adaptin is constitutively de-phosphorylared by serine/threonine protein phosphatase PP2A and phosphorylated by a staurosporine-sensitive kinase. Biochim. Biophys. Acta. 1497:297-307.
    • (2000) Biochim. Biophys. Acta , vol.1497 , pp. 297-307
    • Lauritsen, J.P.1    Menne, C.2    Kastrup, J.3    Dietrich, J.4    Odum, N.5    Geisler, C.6
  • 26
    • 0027371853 scopus 로고
    • Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor
    • Le Borgne, R., A. Schmidt, F. Mauxion, G. Griffiths, and B. Hoflack. 1993. Binding of AP-1 Golgi adaptors to membranes requires phosphorylated cytoplasmic domains of the mannose 6-phosphate/insulin-like growth factor II receptor. J. Biol. Chem. 268:22552-22556.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22552-22556
    • Le Borgne, R.1    Schmidt, A.2    Mauxion, F.3    Griffiths, G.4    Hoflack, B.5
  • 27
    • 0024307676 scopus 로고
    • Phosphorylation/dephosphorylation of the β light chain of clathrin from rat liver coated vesicles
    • Loeb, J.E., B. Cantournet, J.P. Vartanian, J. Goris, and W. Merlevede. 1989. Phosphorylation/dephosphorylation of the β light chain of clathrin from rat liver coated vesicles. Eur. J. Biochem. 182:195-202.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 195-202
    • Loeb, J.E.1    Cantournet, B.2    Vartanian, J.P.3    Goris, J.4    Merlevede, W.5
  • 28
    • 0025598299 scopus 로고
    • Stabilization of clathrin coats by the core of the clathrin-associated protein complex AP-2
    • Matsui, W., and T. Kirchhausen. 1990. Stabilization of clathrin coats by the core of the clathrin-associated protein complex AP-2. Biochemistry. 29:10791-10798.
    • (1990) Biochemistry , vol.29 , pp. 10791-10798
    • Matsui, W.1    Kirchhausen, T.2
  • 29
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion, F., R. Le Borgne, H. Munier-Lehmann, and B. Hoflack. 1996. A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J. Biol. Chem. 271:2171-2178.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 30
    • 0025195684 scopus 로고
    • Phosphorylation of the cytoplasmic domain of the bovine cation-independent mannose 6-phosphate receptor. Serines 2421 and 2492 are the targets of a casein kinase II associated to the Golgi-derived HAI adaptor complex
    • Meresse, S., T. Ludwig, R. Frank, and B. Hoflack. 1990. Phosphorylation of the cytoplasmic domain of the bovine cation-independent mannose 6-phosphate receptor. Serines 2421 and 2492 are the targets of a casein kinase II associated to the Golgi-derived HAI adaptor complex. J. Biol. Chem. 265:18833-18842.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18833-18842
    • Meresse, S.1    Ludwig, T.2    Frank, R.3    Hoflack, B.4
  • 31
    • 0034657033 scopus 로고    scopus 로고
    • μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C., D. Zizioli, S. Lausmann, E.L. Eskelinen, J. Hamann, P. Saftig, K. von Kigura, and P. Schu. 2000. μ1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19:2193-2203.
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Kigura, K.7    Schu, P.8
  • 32
    • 0035691925 scopus 로고    scopus 로고
    • μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate
    • Meyer, C., E.L. Eskelinen, M.R. Guruprasad, K. von Figura, and P. Schu. 2001. μ1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate. J. Cell Sci. 114:4469-4476.
    • (2001) J. Cell Sci. , vol.114 , pp. 4469-4476
    • Meyer, C.1    Eskelinen, E.L.2    Guruprasad, M.R.3    Von Figura, K.4    Schu, P.5
  • 33
    • 0027184670 scopus 로고
    • Purified mammalian HSP-70 KDA activates phosphoprotein phosphatases in vitro
    • Mivechi, N.F., L.D. Trainor, and G.M. Hahn. 1993. Purified mammalian HSP-70 KDA activates phosphoprotein phosphatases in vitro. Biochem. Biophys. Res. Commun. 192:954-963.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 954-963
    • Mivechi, N.F.1    Trainor, L.D.2    Hahn, G.M.3
  • 35
    • 0035950260 scopus 로고    scopus 로고
    • Uncoating of clathrin-coated vesicles in presynaptic terminals: Roles for Hsc70 and auxilin
    • Morgan, J.R., K. Prasad, S. Jin, G.J. Augustine, and E.M. Lafer. 2001. Uncoating of clathrin-coated vesicles in presynaptic terminals: roles for Hsc70 and auxilin. Neuron. 32:289-300.
    • (2001) Neuron , vol.32 , pp. 289-300
    • Morgan, J.R.1    Prasad, K.2    Jin, S.3    Augustine, G.J.4    Lafer, E.M.5
  • 36
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby, M.C., and G. Walter. 1993. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73:673-699.
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 37
    • 0033697037 scopus 로고    scopus 로고
    • A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex
    • Nakagawa, T., M. Setou, D. Seog, K. Ogasawara, N. Dohmae, K. Takio, and N. Hirokawa. 2000. A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex. Cell. 103:569-581.
    • (2000) Cell , vol.103 , pp. 569-581
    • Nakagawa, T.1    Setou, M.2    Seog, D.3    Ogasawara, K.4    Dohmae, N.5    Takio, K.6    Hirokawa, N.7
  • 38
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of ryrosine-based sorting signals
    • Ohno, H., R.C. Aguilar, D. Yeh, D. Taura, T. Saito, and J.S. Bonifacino. 1998. The medium subunits of adaptor complexes recognize distinct but overlapping sets of ryrosine-based sorting signals. J. Biol. Chem. 273:25915-25921.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 39
    • 0035810915 scopus 로고    scopus 로고
    • Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
    • Olusanya, O., P.D. Andrews, J.R. Swedlow, and E. Smythe. 2001. Phosphorylation of threonine 156 of the μ2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo. Curr. Biol. 11:896-900.
    • (2001) Curr. Biol. , vol.11 , pp. 896-900
    • Olusanya, O.1    Andrews, P.D.2    Swedlow, J.R.3    Smythe, E.4
  • 40
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytic signals
    • Owen, D.J., and P.R. Evans. 1998. A structural explanation for the recognition of tyrosine-based endocytic signals. Science. 282:1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 41
    • 0032845769 scopus 로고    scopus 로고
    • γ-synergin: An EH domain-containing protein that interacts with γ-adaptin
    • Page, L.J., P.J. Sowerby, W.W. Lui, and M.S. Robinson. 1999. γ-Synergin: an EH domain-containing protein that interacts with γ-adaptin. J. Cell Biol. 146:993-1004.
    • (1999) J. Cell Biol. , vol.146 , pp. 993-1004
    • Page, L.J.1    Sowerby, P.J.2    Lui, W.W.3    Robinson, M.S.4
  • 42
    • 0030861005 scopus 로고    scopus 로고
    • Platelet adhesion to collagen under flow causes dissociation of a phosphoprotein complex of heat-shock proteins and protein phosphatase 1
    • Polanowska-Grabowska, R., C.G. Simon, Jr., R. Falchetto, J. Shabanowitz, D.F. Hunt, and A.R. Gear. 1997. Platelet adhesion to collagen under flow causes dissociation of a phosphoprotein complex of heat-shock proteins and protein phosphatase 1. Blood. 90:1516-1526.
    • (1997) Blood , vol.90 , pp. 1516-1526
    • Polanowska-Grabowska, R.1    Simon C.G., Jr.2    Falchetto, R.3    Shabanowitz, J.4    Hunt, D.F.5    Gear, A.R.6
  • 43
    • 0027358782 scopus 로고
    • A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase
    • Prasad, K., W. Barouch, L. Greene, and E. Eisenberg. 1993. A protein cofactor is required for uncoating of clathrin baskets by uncoating ATPase. J. Biol. Chem. 268:23758-23761.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23758-23761
    • Prasad, K.1    Barouch, W.2    Greene, L.3    Eisenberg, E.4
  • 45
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport, I., Y.C. Chen, P. Cupers, S.E. Shoelson, and T. Kirchhausen. 1998. Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17:2148-2155.
    • (1998) EMBO J. , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 46
    • 0037018156 scopus 로고    scopus 로고
    • Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals
    • Ricotta, D., S.D. Conner, S.L. Schmid, K. von Figura, and S. Honing. 2002. Phosphorylation of the AP2 μ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J. Cell Biol. 156:791-795.
    • (2002) J. Cell Biol. , vol.156 , pp. 791-795
    • Ricotta, D.1    Conner, S.D.2    Schmid, S.L.3    Von Figura, K.4    Honing, S.5
  • 47
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman, D.M., S.L. Schmid, W.A. Braell, and J.E. Rothman. 1984. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 99:723-733.
    • (1984) J. Cell Biol. , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 48
    • 0036221890 scopus 로고    scopus 로고
    • γ-adaptin interacts directly with Rabaptin-5 through its ear domain
    • Shiba, Y., H. Takatsu, H.W. Shin, and K. Nakayama. 2002. γ-Adaptin interacts directly with Rabaptin-5 through its ear domain. J. Biochem. (Tokyo). 131:327-336.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 327-336
    • Shiba, Y.1    Takatsu, H.2    Shin, H.W.3    Nakayama, K.4
  • 49
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the β2 chain of mammalian AP-2 complexes
    • Shih, W., A. Gallusser, and T. Kirchhausen. 1995. A clathrin-binding site in the hinge of the β2 chain of mammalian AP-2 complexes. J. Biol. Chem. 270:31083-31090.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31083-31090
    • Shih, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 50
    • 0035958856 scopus 로고    scopus 로고
    • Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains
    • Takatsu, H., Y. Katoh, Y. Shiba, and K. Nakayama. 2001. Golgi-localizing, γ-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J. Biol. Chem. 276:28541-28545.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28541-28545
    • Takatsu, H.1    Katoh, Y.2    Shiba, Y.3    Nakayama, K.4
  • 51
    • 0028956745 scopus 로고
    • Different domains of the adaptor protein complex are required for Golgi membrane binding and clathrin recruitment
    • Traub, L.M., S. Kornfeld, and E. Ungewickell. 1995. Different domains of the adaptor protein complex are required for Golgi membrane binding and clathrin recruitment. J. Biol. Chem. 270:4933-4942.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4933-4942
    • Traub, L.M.1    Kornfeld, S.2    Ungewickell, E.3
  • 52
    • 0034118754 scopus 로고    scopus 로고
    • Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation
    • Umeda, A., A. Meyerholz, and E. Ungewickell. 2000. Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation. Eur. J. Cell Biol. 79:336-342.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 336-342
    • Umeda, A.1    Meyerholz, A.2    Ungewickell, E.3
  • 54
    • 0030872085 scopus 로고    scopus 로고
    • Functional interaction of the auxilin J domain with the nucleotide and substrate-binding modules of Hsc70
    • Ungewickell, E., H. Ungewickell, and S.E. Holstein. 1997. Functional interaction of the auxilin J domain with the nucleotide and substrate-binding modules of Hsc70. J. Biol. Chem. 272:19594-19600.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19594-19600
    • Ungewickell, E.1    Ungewickell, H.2    Holstein, S.E.3
  • 56
    • 0029825766 scopus 로고    scopus 로고
    • In vivo phosphorylation of adaptors regulates their interaction with clathrin
    • Wilde, A., and F.M. Brodsky. 1996. In vivo phosphorylation of adaptors regulates their interaction with clathrin. J. Cell Biol. 135:635-645.
    • (1996) J. Cell Biol. , vol.135 , pp. 635-645
    • Wilde, A.1    Brodsky, F.M.2
  • 57
    • 0035128240 scopus 로고    scopus 로고
    • Expression of auxilin of AP180 inhibits endocytosis by mislocalizing clathrin: Evidence for formation of nascent pits containing AP1 or AP2 but not clathrin
    • Zhao, X., T. Greener, H. Al-Hasani, S.W. Cushman, E. Eisenberg, and L.E. Greene. 2001. Expression of auxilin of AP180 inhibits endocytosis by mislocalizing clathrin: evidence for formation of nascent pits containing AP1 or AP2 but not clathrin. J. Cell Sci. 114:353-365.
    • (2001) J. Cell Sci. , vol.114 , pp. 353-365
    • Zhao, X.1    Greener, T.2    Al-Hasani, H.3    Cushman, S.W.4    Eisenberg, E.5    Greene, L.E.6
  • 58
    • 0031843724 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 transiently activates high affinity adaptor protein complex AP-1 binding sites on Golgi membranes
    • Zhu, Y., L.M. Traub, and S. Kornfeld. 1998. ADP-ribosylation factor 1 transiently activates high affinity adaptor protein complex AP-1 binding sites on Golgi membranes. Mol. Biol. Cell. 9:1323-1337.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1323-1337
    • Zhu, Y.1    Traub, L.M.2    Kornfeld, S.3
  • 59
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu, Y., B. Doray, A. Poussu, V.P. Lehto, and S. Kornfeld. 2001. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science. 292:1716-1718.
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5


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