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Volumn 288, Issue 21, 2013, Pages 14788-14804

A role for cargo in Arf-dependent adaptor recruitment

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; CRITICAL COMPONENT; CYTOPLASMIC TAIL; MANNOSE 6 PHOSPHATES; RECYCLING ENDOSOMES; SIGNALING EVENTS; SPECIFIC CONCENTRATION; TRANS-MEMBRANE PROTEINS;

EID: 84878230604     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.453621     Document Type: Article
Times cited : (13)

References (85)
  • 2
    • 0024807217 scopus 로고
    • A novel GTP-binding protein, sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus
    • DOI 10.1083/jcb.109.6.2677
    • Nakańo, A., and Muramatsu, M. (1989) A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109, 2677-2691 (Pubitemid 20011896)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 I , pp. 2677-2691
    • Nakano, A.1    Muramatsu, M.2
  • 3
    • 26244448510 scopus 로고    scopus 로고
    • Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic
    • DOI 10.1091/mbc.E04-12-1042
    • Volpicelli-Daley, L. A., Li, Y., Zhang, C. J., and Kahn, R. A. (2005) Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic. Mol. Biol. Cell 16, 4495-4508 (Pubitemid 41416436)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4495-4508
    • Volpicelli-Daley, L.A.1    Li, Y.2    Zhang, C.-J.3    Kahn, R.A.4
  • 4
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino, J. S., and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem 72, 395-447 (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 5
    • 0036704516 scopus 로고    scopus 로고
    • Cargo selection in vesicular transport: The making and breaking of a coat
    • DOI 10.1034/j.1600-0854.2002.30804.x
    • Aridor, M., and Traub, L. M. (2002) Cargo selection in vesicular transport. The making and breaking of a coat. Traffic 3, 537-546 (Pubitemid 35452891)
    • (2002) Traffic , vol.3 , Issue.8 , pp. 537-546
    • Aridor, M.1    Traub, L.M.2
  • 8
    • 0034607688 scopus 로고    scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5- bisphosphate synthesis in the Golgi compartment
    • DOI 10.1074/jbc.C901019199
    • Jones, D. H., Morris, J. B., Morgan, C. P., Kondo, H., Irvine, R. F., and Cockcroft, S. (2000) Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the golgi compartment. J. Biol. Chem. 275, 13962-13966 (Pubitemid 30257474)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13962-13966
    • Jones, D.H.1    Morris, J.B.2    Morgan, C.P.3    Kondo, H.4    Irvine, R.F.5    Cockcroft, S.6
  • 11
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E., and Orci, L. ( 1992) Molecular dissection of the secretory pathway. Nature 355, 409-415
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 12
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E., and Wieland, F. T. ( 1996) Protein sorting by transport vesicles. Science 272, 227-234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 15
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson, P., and Letourneur, F. ( 1994) Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263, 1629-1631
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 17
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler, K., Veit, M., Stamnes, M. A., and Rothman, J. E. (1996) Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 273, 1396-1399 (Pubitemid 26296529)
    • (1996) Science , vol.273 , Issue.5280 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 18
    • 0037196416 scopus 로고    scopus 로고
    • The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding
    • DOI 10.1016/S0014-5793(01)03299-9, PII S0014579301032999
    • Jacobsen, L., Madsen, P., Nielsen, M. S., Geraerts, W. P., Gliemann, J., Smit, A. B., and Petersen, C. M. (2002) The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding. FEBS Lett. 511, 155-158 (Pubitemid 34127841)
    • (2002) FEBS Letters , vol.511 , Issue.1-3 , pp. 155-158
    • Jacobsen, L.1    Madsen, P.2    Nielsen, M.S.3    Geraerts, W.P.M.4    Gliemann, J.5    Smit, A.B.6    Petersen, C.M.7
  • 19
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg, J. P., Ooi, J., Levy, E., and Margolis, B. (1996) The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on theYENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16, 6229-6241 (Pubitemid 26360983)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.11 , pp. 6229-6241
    • Borg, J.-P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 20
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D. J., and Evans, P. R. (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282, 1327-1332 (Pubitemid 28524497)
    • (1998) Science , vol.282 , Issue.5392 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 21
    • 0030774572 scopus 로고    scopus 로고
    • Functional domain mapping of the clathrin-associated adaptor medium chains μ1 and μ2
    • DOI 10.1074/jbc.272.43.27160
    • Aguilar, R. C., Ohno, H., Roche, K. W., and Bonifacino, J. S. (1997) Functional domain mapping of the clathrin-associated adaptor medium chains μ1 and μ2. J. Biol. Chem. 272, 27160-27166 (Pubitemid 27452674)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 27160-27166
    • Aguilar, R.C.1    Ohno, H.2    Roche, K.W.3    Bonifacino, J.S.4
  • 22
    • 77954382701 scopus 로고    scopus 로고
    • Dynamic structure of membrane-anchored Arf*GTP
    • Liu, Y., Kahn, R. A., and Prestegard, J. H. ( 2010) Dynamic structure of membrane-anchored Arf*GTP. Nat. Struct. Mol. Biol. 17, 876-881
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 876-881
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 23
    • 77953415525 scopus 로고    scopus 로고
    • Modifications to the C terminus of Arf1 alter cell functions and protein interactions
    • Jian, X., Cavenagh, M., Gruschus, J. M., Randazzo, P. A., and Kahn, R. A. ( 2010) Modifications to the C terminus of Arf1 alter cell functions and protein interactions. Traffic 11, 732-742
    • (2010) Traffic , vol.11 , pp. 732-742
    • Jian, X.1    Cavenagh, M.2    Gruschus, J.M.3    Randazzo, P.A.4    Kahn, R.A.5
  • 24
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • DOI 10.1126/science.1075327
    • Doray, B., Ghosh, P., Griffith, J., Geuze, H. J., and Kornfeld, S. (2002) Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297, 1700-1703 (Pubitemid 35000784)
    • (2002) Science , vol.297 , Issue.5587 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 25
    • 0035369294 scopus 로고    scopus 로고
    • Sorting of mannose 6-phosphate receptors mediated by the GGAs
    • DOI 10.1126/science.1060750
    • Puertollano, R., Aguilar, R. C., Gorshkova, I., Crouch, R. J., and Bonifacino, J. S. (2001) Sorting of mannose 6-phosphate receptors mediated by the GGAs. Science 292, 1712-1716 (Pubitemid 32506243)
    • (2001) Science , vol.292 , Issue.5522 , pp. 1712-1716
    • Puertollano, R.1    Aguilar, R.C.2    Gorshkova, I.3    Crouch, R.J.4    Bonifacino, J.S.5
  • 26
    • 0032550222 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles
    • DOI 10.1083/jcb.141.2.359
    • Klumperman, J., Kuliawat, R., Griffith, J. M., Geuze, H. J., and Arvan, P. (1998) Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J. Cell Biol. 141, 359-371 (Pubitemid 28237085)
    • (1998) Journal of Cell Biology , vol.141 , Issue.2 , pp. 359-371
    • Klumperman, J.1    Kuliawat, R.2    Griffith, J.M.3    Geuze, H.J.4    Arvan, P.5
  • 27
    • 0032563130 scopus 로고    scopus 로고
    • Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/γ-adaptin vesicles at the trans-Golgi network
    • DOI 10.1074/jbc.273.30.18966
    • Karlsson, K., and Carlsson, S. R. (1998) Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/γ-adaptin vesicles at the trans-Golgi network. J. Biol. Chem. 273, 18966-18973 (Pubitemid 28366286)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18966-18973
    • Karlsson, K.1    Carlsson, S.R.2
  • 28
    • 0024241414 scopus 로고
    • Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles
    • DOI 10.1083/jcb.107.6.2491
    • Geuze, H. J., Stoorvogel, W., Strous, G. J., Slot, J. W., Bleekemolen, J. E., and Mellman, I. (1988) Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles. J. Cell Biol. 107, 2491-2501 (Pubitemid 19019395)
    • (1988) Journal of Cell Biology , vol.107 , Issue.6 II , pp. 2491-2501
    • Geuze, H.J.1    Stoorvogel, W.2    Strous, G.J.3    Slot, J.W.4    Bleekemolen, J.E.5    Mellman, I.6
  • 29
    • 2442530398 scopus 로고    scopus 로고
    • Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor
    • DOI 10.1083/jcb.200312055
    • Arighi, C. N., Hartnell, L. M., Aguilar, R. C., Haft, C. R., and Bonifacino, J. S. (2004) Role of the mammalian retromer in sorting of the cation-independent mannose 6-phosphate receptor. J. Cell Biol. 165, 123-133 (Pubitemid 38649182)
    • (2004) Journal of Cell Biology , vol.165 , Issue.1 , pp. 123-133
    • Arighi, C.N.1    Harmell, L.M.2    Aguilar, R.C.3    Haft, C.R.4    Bonifacino, J.S.5
  • 30
    • 0034252326 scopus 로고    scopus 로고
    • The dileucine motif within the tail of MPR46 is required for sorting of the receptor in endosomes
    • Tikkanen, R., Obermüller, S., Denzer, K., Pungitore, R., Geuze, H. J., von Figura, K., and Höning, S. ( 2000) The dileucine motif within the tail of MPR46 is required for sorting of the receptor in endosomes. Traffic 1, 631-640
    • (2000) Traffic , vol.1 , pp. 631-640
    • Tikkanen, R.1    Obermüller, S.2    Denzer, K.3    Pungitore, R.4    Geuze, H.J.5    Von Figura, K.6    Höning, S.7
  • 31
    • 34247343328 scopus 로고    scopus 로고
    • The role of cargo proteins in GGA recruitment
    • DOI 10.1111/j.1600-0854.2007.00556.x
    • Hirst, J., Seaman, M. N., Buschow, S. I., and Robinson, M. S. (2007) The role of cargo proteins in GGA recruitment. Traffic 8, 594-604 (Pubitemid 46638567)
    • (2007) Traffic , vol.8 , Issue.5 , pp. 594-604
    • Hirst, J.1    Seaman, M.N.J.2    Buschow, S.I.3    Robinson, M.S.4
  • 32
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge. from protein traffic to embryogenesis and disease
    • Thomas, G. ( 2002) Furin at the cutting edge. from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3, 753-766
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 33
    • 0040142226 scopus 로고    scopus 로고
    • Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins
    • Teuchert, M., Schäfer, W., Berghöfer, S., Hoflack, B., Klenk, H. D., and Garten, W. ( 1999) Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins. J. Biol. Chem. 274, 8199-8207
    • (1999) J. Biol. Chem. , vol.274 , pp. 8199-8207
    • Teuchert, M.1    Schäfer, W.2    Berghöfer, S.3    Hoflack, B.4    Klenk, H.D.5    Garten, W.6
  • 34
    • 48049087904 scopus 로고    scopus 로고
    • Interaction of Mint3 with furin regulates the localization of furin in the trans-Golgi network
    • Han, J., Wang, Y., Wang, S., and Chi, C. ( 2008) Interaction of Mint3 with furin regulates the localization of furin in the trans-Golgi network. J. Cell Sci. 121, 2217-2223
    • (2008) J. Cell Sci. , vol.121 , pp. 2217-2223
    • Han, J.1    Wang, Y.2    Wang, S.3    Chi, C.4
  • 35
    • 0022187987 scopus 로고
    • Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane
    • DOI 10.1083/jcb.101.3.949
    • Griffiths, G., Pfeiffer, S., Simons, K., and Matlin, K. (1985) Exit of newly synthesized membrane proteins from the trans cisterna of the Golgi complex to the plasma membrane. J. Cell Biol. 101, 949-964 (Pubitemid 16258222)
    • (1985) Journal of Cell Biology , vol.101 , Issue.3 , pp. 949-964
    • Griffiths, G.1    Pfeiffer, S.2    Simons, K.3    Matlin, K.4
  • 36
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments
    • Ladinsky, M. S., Wu, C. C., McIntosh, S., McIntosh, J. R., and Howell, K. E. ( 2002) Structure of the Golgi and distribution of reporter molecules at 20°C reveals the complexity of the exit compartments. Mol. Biol. Cell 13, 2810-2825
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.C.2    McIntosh, S.3    McIntosh, J.R.4    Howell, K.E.5
  • 37
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin, K. S., and Simons, K. ( 1983) Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell 34, 233-243
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 39
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson, J. G., Lippincott-Schwartz, J., Bloom, G. S., Kreis, T. E., and Klausner, R. D. (1990) Dissociation of a 110-kDa peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J. Cell Biol. 111, 2295-2306 (Pubitemid 120014515)
    • (1990) Journal of Cell Biology , vol.111 , Issue.6 PART 1 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 40
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER
    • DOI 10.1016/0092-8674(89)90685-5
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S., and Klausner, R. D. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A. Evidence for membrane cycling from Golgi to ER. Cell 56, 801-813 (Pubitemid 19082516)
    • (1989) Cell , vol.56 , Issue.5 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 41
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • DOI 10.1083/jcb.123.3.561
    • Traub, L. M., Ostrom, J. A., and Kornfeld, S. (1993) Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123, 561-573 (Pubitemid 23324914)
    • (1993) Journal of Cell Biology , vol.123 , Issue.3 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 42
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase. Localization to the TGN and recycling from the cell surface
    • Molloy, S. S., Thomas, L., VanSlyke, J. K., Stenberg, P. E., and Thomas, G. ( 1994) Intracellular trafficking and activation of the furin proprotein convertase. Localization to the TGN and recycling from the cell surface. EMBO J. 13, 18-33
    • (1994) EMBO J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 44
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • DOI 10.1111/j.1365-2818.2006.01706.x
    • Bolte, S., and Cordelières, F. P. (2006) A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213-232 (Pubitemid 46010930)
    • (2006) Journal of Microscopy , vol.224 , Issue.3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 45
    • 29944435174 scopus 로고    scopus 로고
    • Seeing is believing? A beginners guide to practical pitfalls in image acquisition
    • North, A. J. ( 2006) Seeing is believing? A beginners guide to practical pitfalls in image acquisition. J. Cell Biol. 172, 9-18
    • (2006) J. Cell Biol. , vol.172 , pp. 9-18
    • North, A.J.1
  • 46
    • 84878215455 scopus 로고    scopus 로고
    • Computational method for calculating fluorescence intensities within three-dimensional structures in cells
    • Caster, A. H., and Kahn, R. A. ( 2012) Computational method for calculating fluorescence intensities within three-dimensional structures in cells. Cell. Logist. 2, 176-188
    • (2012) Cell. Logist. , vol.2 , pp. 176-188
    • Caster, A.H.1    Kahn, R.A.2
  • 47
    • 34547796509 scopus 로고    scopus 로고
    • Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval
    • Seaman, M. N. ( 2007) Identification of a novel conserved sorting motif required for retromer-mediated endosome-to-TGN retrieval. J. Cell Sci. 120, 2378-2389
    • (2007) J. Cell Sci. , vol.120 , pp. 2378-2389
    • Seaman, M.N.1
  • 48
    • 2442509574 scopus 로고    scopus 로고
    • Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer
    • Seaman, M. N. ( 2004) Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer. J. Cell Biol. 165, 111-122
    • (2004) J. Cell Biol. , vol.165 , pp. 111-122
    • Seaman, M.N.1
  • 49
    • 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., Katoh, Y., Shiba, Y., and Nakayama, K. ( 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
  • 50
    • 0029791503 scopus 로고    scopus 로고
    • The tyrosine-based lysosomal targeting signal in lamp-1 mediates sorting into Golgi-derived clathrin-coated vesicles
    • Höning, S., Griffith, J., Geuze, H. J., and Hunziker, W. (1996) The tyrosine-based lysosomal targeting signal in lamp-1 mediates sorting into Golgiderived clathrin-coated vesicles. EMBO J. 15, 5230-5239 (Pubitemid 26336206)
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5230-5239
    • Honing, S.1    Griffith, J.2    Geuze, H.J.3    Hunziker, W.4
  • 51
    • 0029935911 scopus 로고    scopus 로고
    • In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting
    • Heilker, R., Manning-Krieg, U., Zuber, J. F., and Spiess, M. (1996) In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J. 15, 2893-2899 (Pubitemid 26176267)
    • (1996) EMBO Journal , vol.15 , Issue.11 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg, U.2    Zuber, J.-F.3    Spiess, M.4
  • 52
    • 0021148465 scopus 로고
    • Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface
    • Saraste, J., and Kuismanen, E. (1984) Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface. Cell 38, 535-549 (Pubitemid 14022046)
    • (1984) Cell , vol.38 , Issue.2 , pp. 535-549
    • Saraste, J.1    Kuismanen, E.2
  • 53
    • 0022456633 scopus 로고
    • Reduced temperature can block different glycoproteins at different steps during transport to the plasma membrane
    • Mottet, G., Tuffereau, C., and Roux, L. (1986) Reduced temperature can block different glycoproteins at different steps during transport to the plasma membrane. J. Gen. Virol. 67, 2029-2035 (Pubitemid 16017290)
    • (1986) Journal of General Virology , vol.67 , Issue.9 , pp. 2029-2035
    • Mottet, G.1    Tuffereau, C.2    Roux, L.3
  • 54
    • 0020611460 scopus 로고
    • Reversible block in intracellular transport and budding of mutant vesicular stomatitis virus glycoproteins
    • Lodish, H. F., and Kong, N. (1983) Reversible block in intracellular transport and budding of mutant vesicular stomatitis virus glycoproteins. Virology 125, 335-348 (Pubitemid 13120111)
    • (1983) Virology , vol.125 , Issue.2 , pp. 335-348
    • Lodish, H.F.1    Kong, N.2
  • 55
    • 2542449272 scopus 로고    scopus 로고
    • The cytoplasmic tail of the cation-independent mannose 6-phosphate receptor contains four binding sites for AP-1
    • DOI 10.1016/j.abb.2004.02.011, PII S0003986104000864
    • Ghosh, P., and Kornfeld, S. (2004) The cytoplasmic tail of the cation-independent mannose 6-phosphate receptor contains four binding sites for AP-1. Arch Biochem. Biophys. 426, 225-230 (Pubitemid 38680619)
    • (2004) Archives of Biochemistry and Biophysics , vol.426 , Issue.2 , pp. 225-230
    • Ghosh, P.1    Kornfeld, S.2
  • 57
    • 0025943380 scopus 로고
    • Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S. A., Park, J. E., and Brown, W. J. (1991) Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes. Cell 67, 591-600 (Pubitemid 121001473)
    • (1991) Cell , vol.67 , Issue.3 , pp. 591-600
    • Wood, S.A.1    Park, J.E.2    Brown, W.J.3
  • 59
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • DOI 10.1083/jcb.137.6.1255
    • Odorizzi, G., and Trowbridge, I. S. (1997) Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J. Cell Biol. 137, 1255-1264 (Pubitemid 27265940)
    • (1997) Journal of Cell Biology , vol.137 , Issue.6 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 61
    • 0034036097 scopus 로고    scopus 로고
    • A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi
    • Boman, A. L., Zhang, C. j., Zhu, X., and Kahn, R. A. (2000) A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol. Biol. Cell 11, 1241-1255 (Pubitemid 30211027)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.4 , pp. 1241-1255
    • Boman, A.L.1    Zhang, C.-J.2    Zhu, X.3    Kahn, R.A.4
  • 62
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with γ-adaptin and VHS domains that facilitates trafficking between the trans-Golgi network and the vacuole/lysosome
    • Hirst, J., Lui, W. W., Bright, N. A., Totty, N., Seaman, M. N., and Robinson, M. S. ( 2000) A family of proteins with γ-adaptin and VHS domains that facilitates trafficking between the trans-Golgi network and the vacuole/lysosome. J. Cell Biol. 149, 67-80
    • (2000) J. Cell Biol. , vol.149 , pp. 67-80
    • Hirst, J.1    Lui, W.W.2    Bright, N.A.3    Totty, N.4    Seaman, M.N.5    Robinson, M.S.6
  • 63
    • 0034797505 scopus 로고    scopus 로고
    • Assays of ADP-ribosylation factor function
    • Kuai, J., and Kahn, R. A. ( 2002) Assays of ADP-ribosylation factor function. Methods Enzymol. 345, 359-370
    • (2002) Methods Enzymol. , vol.345 , pp. 359-370
    • Kuai, J.1    Kahn, R.A.2
  • 64
    • 30544440892 scopus 로고    scopus 로고
    • Analysis of Arf interaction with GGAs in vitro and in vivo
    • Nakayama, K., and Takatsu, H. ( 2005) Analysis of Arf interaction with GGAs in vitro and in vivo. Methods Enzymol. 404, 367-377
    • (2005) Methods Enzymol. , vol.404 , pp. 367-377
    • Nakayama, K.1    Takatsu, H.2
  • 65
    • 30544436453 scopus 로고    scopus 로고
    • In vitro assays of Arf1 interaction with GGA proteins
    • DOI 10.1016/S0076-6879(05)04028-0, PII S0076687905040280, 28, GTPases Regulating Membrane Dynamics
    • Yoon, H. Y., Bonifacino, J. S., and Randazzo, P. A. (2005) In vitro assays of Arf1 interaction with GGA proteins. Methods Enzymol. 404, 316-332 (Pubitemid 43081994)
    • (2006) Methods in Enzymology , vol.404 , pp. 316-332
    • Yoon, H.-Y.1    Bonifacino, J.S.2    Randazzo, P.A.3
  • 67
    • 79953777161 scopus 로고    scopus 로고
    • Decoupling of activation and effector binding underlies ARF6 priming of fast endocytic recycling
    • Montagnac, G., de Forges, H., Smythe, E., Gueudry, C., Romao, M., Salamero, J., and Chavrier, P. ( 2011) Decoupling of activation and effector binding underlies ARF6 priming of fast endocytic recycling. Curr. Biol. 21, 574-579
    • (2011) Curr. Biol. , vol.21 , pp. 574-579
    • Montagnac, G.1    De Forges, H.2    Smythe, E.3    Gueudry, C.4    Romao, M.5    Salamero, J.6    Chavrier, P.7
  • 68
    • 0032076636 scopus 로고    scopus 로고
    • Tip47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • DOI 10.1016/S0092-8674(00)81171-X
    • Díaz, E., and Pfeffer, S. R. (1998) TIP47. A cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93, 433-443 (Pubitemid 28232087)
    • (1998) Cell , vol.93 , Issue.3 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 69
    • 0242363236 scopus 로고    scopus 로고
    • Characterization of the in vitro retrograde transport of MPR46
    • DOI 10.1034/j.1600-0854.2003.00136.x
    • Medigeshi, G. R., and Schu, P. (2003) Characterization of the in vitro retrograde transport of MPR46. Traffic 4, 802-811 (Pubitemid 37361859)
    • (2003) Traffic , vol.4 , Issue.11 , pp. 802-811
    • Medigeshi, G.R.1    Schu, P.2
  • 70
    • 0034685644 scopus 로고    scopus 로고
    • Adaptor γ ear homology domain conserved in γ-adaptin and GGA proteins that interact with γ-synergin
    • DOI 10.1006/bbrc.2000.2700
    • Takatsu, H., Yoshino, K., and Nakayama, K. (2000) Adaptor γ ear homology domain conserved in γ-adaptin and GGA proteins that interact with γ-synergin. Biochem. Biophys. Res. Commun. 271, 719-725 (Pubitemid 30444695)
    • (2000) Biochemical and Biophysical Research Communications , vol.271 , Issue.3 , pp. 719-725
    • Takatsu, H.1    Yoshino, K.2    Nakayama, K.3
  • 72
    • 34247623568 scopus 로고    scopus 로고
    • Coats, Tethers, Rabs, and SNAREs Work Together to Mediate the Intracellular Destination of a Transport Vesicle
    • DOI 10.1016/j.devcel.2007.04.005, PII S1534580707001529
    • Cai, H., Reinisch, K., and Ferro-Novick, S. (2007) Coats, tethers, Rabs, and SNARES work together to mediate the intracellular destination of a transport vesicle. Dev. Cell 12, 671-682 (Pubitemid 46667749)
    • (2007) Developmental Cell , vol.12 , Issue.5 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 73
    • 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., Schmidt, A., Mauxion, F., Griffiths, G., and Hoflack, B. (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 (Pubitemid 23318309)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22552-22556
    • Le, B.R.1    Schmidt, A.2    Mauxion, F.3    Griffiths, G.4    Hoflack, B.5
  • 74
    • 0036199384 scopus 로고    scopus 로고
    • The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins
    • DOI 10.1016/S1534-5807(02)00127-2
    • Valdivia, R. H., Baggott, D., Chuang, J. S., and Schekman, R. W. (2002) The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev. Cell 2, 283-294 (Pubitemid 34266114)
    • (2002) Developmental Cell , vol.2 , Issue.3 , pp. 283-294
    • Valdivia, R.H.1    Baggott, D.2    Chuang, J.S.3    Schekman, R.W.4
  • 75
    • 0034657033 scopus 로고    scopus 로고
    • μ1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C., Zizioli, D., Lausmann, S., Eskelinen, E. L., Hamann, J., Saftig, P., von Figura, K., and Schu, P. (2000) μ1A-adaptin-deficient mice. Lethality, loss of AP-1 binding, and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193-2203 (Pubitemid 30259000)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.-L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 76
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of Shiga toxin B-fragment transport
    • DOI 10.1083/jcb.143.4.973
    • Mallard, F., Antony, C., Tenza, D., Salamero, J., Goud, B., and Johannes, L. (1998) Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 143, 973-990 (Pubitemid 28547397)
    • (1998) Journal of Cell Biology , vol.143 , Issue.4 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 77
    • 20444377260 scopus 로고    scopus 로고
    • GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network
    • DOI 10.1016/j.mcn.2005.03.014, PII S1044743105000734
    • Wahle, T., Prager, K., Raffler, N., Haass, C., Famulok, M., and Walter, J. (2005) GGA proteins regulate retrograde transport of BACE1 from endosomes to the trans-Golgi network. Mol. Cell. Neurosci. 29, 453-461 (Pubitemid 40799217)
    • (2005) Molecular and Cellular Neuroscience , vol.29 , Issue.3 , pp. 453-461
    • Wahle, T.1    Prager, K.2    Raffler, N.3    Haass, C.4    Famulok, M.5    Walter, J.6
  • 78
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano, R., and Bonifacino, J. S. (2004) Interactions of GGA3 with the ubiquitin sorting machinery. Nat. Cell Biol. 6, 244-251 (Pubitemid 38344363)
    • (2004) Nature Cell Biology , vol.6 , Issue.3 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 79
    • 15744380393 scopus 로고    scopus 로고
    • GGA proteins mediate the recycling pathway of memapsin 2 (BACE)
    • DOI 10.1074/jbc.M411296200
    • He, X., Li, F., Chang, W.-P., and Tang, J. (2005) GGA proteins mediate the recycling pathway of memapsin 2 (BACE). J. Biol. Chem. 280, 11696-11703 (Pubitemid 40418483)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11696-11703
    • He, X.1    Li, F.2    Chang, W.-P.3    Tang, J.4
  • 82
    • 1042292020 scopus 로고    scopus 로고
    • Multiple phosphorylation events regulate the subcellular localization of GGA1
    • DOI 10.1111/j.1600-0854.2004.00160.x
    • McKay, M. M., and Kahn, R. A. (2004) Multiple phosphorylation events regulate the subcellular localization of GGA1. Traffic 5, 102-116 (Pubitemid 38196022)
    • (2004) Traffic , vol.5 , Issue.2 , pp. 102-116
    • McKay, M.M.1    Kahn, R.A.2
  • 85
    • 0030497711 scopus 로고    scopus 로고
    • Rab proteins in gastric parietal cells: Evidence for the membrane recycling hypothesis
    • Calhoun, B. C., and Goldenring, J. R. (1996) Rab proteins in gastric parietal cells. Evidence for the membrane recycling hypothesis. Yale J. Biol. Med. 69, 1-8 (Pubitemid 27076704)
    • (1996) Yale Journal of Biology and Medicine , vol.69 , Issue.1 , pp. 1-8
    • Calhoun, B.C.1    Goldenring, J.R.2


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