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Volumn 17, Issue 4, 2006, Pages 1845-1858

The Gcs1 Arf-GAP mediates Snc1,2 v-SNAKE retrieval to the Golgi in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; COATOMER PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RECOMBINANT PROTEIN; SNARE PROTEIN; FUNGAL PROTEIN; SYNAPTOBREVIN;

EID: 33745413038     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-09-0832     Document Type: Article
Times cited : (70)

References (69)
  • 1
    • 0032496164 scopus 로고    scopus 로고
    • Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures
    • Abeliovich, H., Grote, E., Novick, P., and Ferro-Novick, S. (1998). Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. J. Biol. Chem. 273, 11719-11727.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11719-11727
    • Abeliovich, H.1    Grote, E.2    Novick, P.3    Ferro-Novick, S.4
  • 2
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F., Gu, F., Parton, R. G., and Gruenberg, J. (1996). An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes. J. Cell Biol. 133, 29-41.
    • (1996) J. Cell Biol. , vol.133 , pp. 29-41
    • Aniento, F.1    Gu, F.2    Parton, R.G.3    Gruenberg, J.4
  • 3
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay, J., Gounon, P., Robineau, S., and Antonny, B. (2003). Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426, 563-566.
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4
  • 4
    • 0028030275 scopus 로고
    • Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis
    • Brennwald, P., Kearns, B., Champion, K., Keranen, S., Bankaitis, V., and Novick, P. (1994). Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79, 245-258.
    • (1994) Cell , vol.79 , pp. 245-258
    • Brennwald, P.1    Kearns, B.2    Champion, K.3    Keranen, S.4    Bankaitis, V.5    Novick, P.6
  • 5
    • 0038360874 scopus 로고    scopus 로고
    • The Sec1p/Munc18 (SM) protein, Vps45p, cycles on and off membranes during vesicle transport
    • Bryant, N. J., and James, D. E. (2003). The Sec1p/Munc18 (SM) protein, Vps45p, cycles on and off membranes during vesicle transport. J. Cell Biol. 163, 691-696.
    • (2003) J. Cell Biol. , vol.163 , pp. 691-696
    • Bryant, N.J.1    James, D.E.2
  • 6
    • 12744281102 scopus 로고    scopus 로고
    • Sorting nexins-unifying trends and new perspectives
    • Carlton, J., Bujny, M., Rutherford, A., and Cullen, P. (2005). Sorting nexins-unifying trends and new perspectives. Traffic 6, 75-82.
    • (2005) Traffic , vol.6 , pp. 75-82
    • Carlton, J.1    Bujny, M.2    Rutherford, A.3    Cullen, P.4
  • 7
    • 11144333620 scopus 로고    scopus 로고
    • Ypt31/32 GTPases and their novel F-box effector protein Rcy1 regulate protein recycling
    • Chen, S. H., Chen, S., Tokarev, A. A., Liu, F., Jedd, G., and Segev, N. (2005). Ypt31/32 GTPases and their novel F-box effector protein Rcy1 regulate protein recycling. Mol. Biol. Cell 36, 178-192.
    • (2005) Mol. Biol. Cell , vol.36 , pp. 178-192
    • Chen, S.H.1    Chen, S.2    Tokarev, A.A.3    Liu, F.4    Jedd, G.5    Segev, N.6
  • 9
    • 0027992040 scopus 로고
    • Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins
    • Couve, A., and Gerst, J. E. (1994). Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins. J. Biol. Chem. 269, 23391-23394.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23391-23394
    • Couve, A.1    Gerst, J.E.2
  • 10
    • 0029042360 scopus 로고
    • Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate
    • Couve, A., Protopopov, V., and Gerst, J. E. (1995). Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate. Proc. Natl. Acad. Sci. USA 92, 5987-5991.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5987-5991
    • Couve, A.1    Protopopov, V.2    Gerst, J.E.3
  • 12
    • 0034254166 scopus 로고    scopus 로고
    • COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP
    • Eugster, A., Frigerio, G., Dale, M., and Duden, R. (2000). COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP. EMBO J. 39, 3905-3917.
    • (2000) EMBO J. , vol.39 , pp. 3905-3917
    • Eugster, A.1    Frigerio, G.2    Dale, M.3    Duden, R.4
  • 13
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T., and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 15
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., Redding, K., Crosby, J., Fuller, R. S., and Schekman, R. (1991). Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 312, 27-37.
    • (1991) J. Cell Biol. , vol.312 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 17
    • 0030959248 scopus 로고    scopus 로고
    • Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function
    • Gerst, J. E. (1997). Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function. J. Biol. Chem. 272, 16591-16598.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16591-16598
    • Gerst, J.E.1
  • 18
    • 0026556288 scopus 로고
    • SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: Genetic interactions with the RAS and CAP genes
    • Gerst, J. E., Rodgers, L., Riggs, M., and Wigler, M. (1992). SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genes. Proc. Natl. Acad. Sci. USA 89, 4338-4342.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4338-4342
    • Gerst, J.E.1    Rodgers, L.2    Riggs, M.3    Wigler, M.4
  • 19
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein, A. L., and McCusker, J. H. (1999). Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 35, 1541-1553.
    • (1999) Yeast , vol.35 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 21
    • 0034678130 scopus 로고    scopus 로고
    • ARF1 regulates pH-dependent COP functions in the early endocytic pathway
    • Gu, F., and Gruenberg, J. (2000). ARF1 regulates pH-dependent COP functions in the early endocytic pathway. J. Biol. Chem. 275, 8154-8160.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8154-8160
    • Gu, F.1    Gruenberg, J.2
  • 23
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick, K. G., and Pelham, H. R. (1992). SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J. Cell Biol. 119, 513-521.
    • (1992) J. Cell Biol. , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.2
  • 24
    • 0027499194 scopus 로고
    • Effect of myristoylation on GTP-dependent binding of ADP-ribosylation factor to Golgi
    • Haun, R. S., Tsai, S. C., Adamik, R., Moss, J., and Vaughan, M. (1993). Effect of myristoylation on GTP-dependent binding of ADP-ribosylation factor to Golgi. J. Biol. Chem. 268, 7064-7068.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7064-7068
    • Haun, R.S.1    Tsai, S.C.2    Adamik, R.3    Moss, J.4    Vaughan, M.5
  • 25
    • 0037415752 scopus 로고    scopus 로고
    • Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes
    • Hettema, E. H., Lewis, M. J., Black, M. W., and Pelham, H. R. (2003). Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval pathways from yeast endosomes. EMBO J. 22, 548-557.
    • (2003) EMBO J. , vol.22 , pp. 548-557
    • Hettema, E.H.1    Lewis, M.J.2    Black, M.W.3    Pelham, H.R.4
  • 26
    • 0141527343 scopus 로고    scopus 로고
    • Conserved structural motifs in intracellular trafficking pathways: Structure of the gammaCOP appendage domain
    • Hoffman, G. R., Rahl, P. B., Collins, R. N., and Cerione, R. A. (2003). Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain. Mol. Cell 12, 615-625.
    • (2003) Mol. Cell , vol.12 , pp. 615-625
    • Hoffman, G.R.1    Rahl, P.B.2    Collins, R.N.3    Cerione, R.A.4
  • 27
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis, J. C., Nichols, B. J., Dhruvakumar, S., and Pelham, H. R. (1998). Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 17, 113-126.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.4
  • 28
    • 0026620198 scopus 로고
    • SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer
    • Hosobuchi, M., Kreis, T., and Schekman, R. (1992). SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer. Nature 360, 603-605.
    • (1992) Nature , vol.360 , pp. 603-605
    • Hosobuchi, M.1    Kreis, T.2    Schekman, R.3
  • 29
    • 0028017275 scopus 로고
    • A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation
    • Ireland, L. S., Johnston, G. C., Drebot, M. A., Dhillon, N., DeMaggio, A. J., Hoekstra, M. F., and Singer, R. A. (1994). A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. EMBO J. 13, 3812-3821.
    • (1994) EMBO J. , vol.13 , pp. 3812-3821
    • Ireland, L.S.1    Johnston, G.C.2    Drebot, M.A.3    Dhillon, N.4    Demaggio, A.J.5    Hoekstra, M.F.6    Singer, R.A.7
  • 31
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
    • Jedd, G., Mulholland, J., and Segev, N. (1997). Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment. J. Cell Biol. 137, 563-580.
    • (1997) J. Cell Biol. , vol.137 , pp. 563-580
    • Jedd, G.1    Mulholland, J.2    Segev, N.3
  • 32
    • 0035825175 scopus 로고    scopus 로고
    • Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex
    • Kim, J., Huang, W. P., and Klionsky, D. J. (2001). Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex. J. Cell Biol. 152, 51-64.
    • (2001) J. Cell Biol. , vol.152 , pp. 51-64
    • Kim, J.1    Huang, W.P.2    Klionsky, D.J.3
  • 35
    • 1942453869 scopus 로고    scopus 로고
    • The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p
    • Lafourcade, C., Galan, J. M., Gloor, Y., Haguenauer-Tsapis, R., and Peter, M. (2004). The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p. Mol. Cell Biol. 24, 3815-3826.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3815-3826
    • Lafourcade, C.1    Galan, J.M.2    Gloor, Y.3    Haguenauer-Tsapis, R.4    Peter, M.5
  • 36
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAP1
    • Lanoix, J., Ouwendijk, J., Stark, A., Szafer, E., Cassel, D., Dejgaard, K., Weiss, M., and Nilsson, T. (2001). Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J. Cell Biol. 155, 1199-1212.
    • (2001) J. Cell Biol. , vol.155 , pp. 1199-1212
    • Lanoix, J.1    Ouwendijk, J.2    Stark, A.3    Szafer, E.4    Cassel, D.5    Dejgaard, K.6    Weiss, M.7    Nilsson, T.8
  • 39
    • 4344568212 scopus 로고    scopus 로고
    • The ArfGAP Glo3 is required for the generation of COPI vesicles
    • Lewis, S. M., Poon, P. P., Singer, R. A., Johnston, G. C., and Spang, A. (2004). The ArfGAP Glo3 is required for the generation of COPI vesicles. Mol. Biol. Cell 15, 4064-4072.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4064-4072
    • Lewis, S.M.1    Poon, P.P.2    Singer, R.A.3    Johnston, G.C.4    Spang, A.5
  • 40
    • 0033006355 scopus 로고    scopus 로고
    • Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis
    • Lustgarten, V., and Gerst, J. E. (1999). Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Mol. Cell Biol. 19, 4480-4494.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4480-4494
    • Lustgarten, V.1    Gerst, J.E.2
  • 41
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam, J., Satoh, A., Pelletier, L., and Warren, G. (2005). Golgin tethers define subpopulations of COPI vesicles. Science 307, 1095-1098.
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 42
    • 0034282521 scopus 로고    scopus 로고
    • A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting
    • Matern, H., Yang, X., Andrulis, E., Sternglanz, R., Trepte, H. H., and Gallwitz, D. (2000). A novel Golgi membrane protein is part of a GTPase-binding protein complex involved in vesicle targeting. EMBO J. 19, 4485-4492.
    • (2000) EMBO J. , vol.19 , pp. 4485-4492
    • Matern, H.1    Yang, X.2    Andrulis, E.3    Sternglanz, R.4    Trepte, H.H.5    Gallwitz, D.6
  • 43
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • McMahon, H. T., and Mills, I. G. (2004). COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr. Opin. Cell Biol. 16, 379-391.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 44
    • 0031738937 scopus 로고    scopus 로고
    • Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPgammaS in vitro
    • Nickel, W., Malsam, J., Gorgas, K., Ravazzola, M., Jenne, N., Helms, J. B., and Wieland, F. T. (1998). Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPgammaS in vitro. J. Cell Sci. 111, 3081-3090.
    • (1998) J. Cell Sci. , vol.111 , pp. 3081-3090
    • Nickel, W.1    Malsam, J.2    Gorgas, K.3    Ravazzola, M.4    Jenne, N.5    Helms, J.B.6    Wieland, F.T.7
  • 46
    • 0033979448 scopus 로고    scopus 로고
    • COPI vesicles accumulating in the presence of a GTP restricted arf1 mutant are depleted of anterograde and retrograde cargo
    • Pepperkok, R., Whitney, J. A., Gomez, M., and Kreis, T. E. (2000). COPI vesicles accumulating in the presence of a GTP restricted arf1 mutant are depleted of anterograde and retrograde cargo. J. Cell Sci. 213, 135-144.
    • (2000) J. Cell Sci. , vol.213 , pp. 135-144
    • Pepperkok, R.1    Whitney, J.A.2    Gomez, M.3    Kreis, T.E.4
  • 47
    • 0033081078 scopus 로고    scopus 로고
    • Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function
    • Poon, P. P., Cassel, D., Spang, A., Rotman, M., Pick, E., Singer, R. A., and Johnston, G. C. (1999). Retrograde transport from the yeast Golgi is mediated by two ARF GAP proteins with overlapping function. EMBO J. 18, 555-564.
    • (1999) EMBO J. , vol.18 , pp. 555-564
    • Poon, P.P.1    Cassel, D.2    Spang, A.3    Rotman, M.4    Pick, E.5    Singer, R.A.6    Johnston, G.C.7
  • 48
    • 0035945364 scopus 로고    scopus 로고
    • The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network
    • Poon, P. P., Nothwehr, S. F., Singer, R. A., and Johnston, G. C. (2001). The Gcs1 and Age2 ArfGAP proteins provide overlapping essential function for transport from the yeast trans-Golgi network. J. Cell Biol. 155, 1239-1250.
    • (2001) J. Cell Biol. , vol.155 , pp. 1239-1250
    • Poon, P.P.1    Nothwehr, S.F.2    Singer, R.A.3    Johnston, G.C.4
  • 50
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., Govindan, B., Novick, P., and Gerst, J. E. (1993). Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell 74, 855-861.
    • (1993) Cell , vol.74 , pp. 855-861
    • Protopopov, V.1    Govindan, B.2    Novick, P.3    Gerst, J.E.4
  • 51
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling
    • Randazzo, P. A., and Hirsch, D. S. (2004). Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell Signal. 16, 401-413.
    • (2004) Cell Signal. , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 52
    • 0037193471 scopus 로고    scopus 로고
    • ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
    • Rein, U., Andag, U., Duden, R., Schmitt, H. D., and Spang, A. (2002). ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat. J. Cell Biol. 157, 395-404.
    • (2002) J. Cell Biol. , vol.157 , pp. 395-404
    • Rein, U.1    Andag, U.2    Duden, R.3    Schmitt, H.D.4    Spang, A.5
  • 54
    • 0038492465 scopus 로고    scopus 로고
    • Functional reconstitution of COPI coat assembly and disassembly using chemically defined components
    • Reinhard, C., Schweikert, M., Wieland, F. T., and Nickel, W. (2003). Functional reconstitution of COPI coat assembly and disassembly using chemically defined components. Proc. Natl. Acad. Sci. USA 100, 8253-8257.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8253-8257
    • Reinhard, C.1    Schweikert, M.2    Wieland, F.T.3    Nickel, W.4
  • 56
    • 0031694848 scopus 로고    scopus 로고
    • A yeast t-SNARE involved in endocytosis
    • Seron, K., et al. (1998). A yeast t-SNARE involved in endocytosis. Mol. Biol. Cell 9, 2873-2889.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2873-2889
    • Seron, K.1
  • 57
    • 0028221677 scopus 로고
    • A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferase
    • Sharrocks, A. D. (1994). A T7 expression vector for producing N- and C-terminal fusion proteins with glutathione S-transferase. Gene 138, 105-108.
    • (1994) Gene , vol.138 , pp. 105-108
    • Sharrocks, A.D.1
  • 58
    • 0034665261 scopus 로고    scopus 로고
    • Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p
    • Siniossoglou, S., Peak-Chew, S. Y., and Pelham, H. R. (2000). Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J. 19, 4885-4894.
    • (2000) EMBO J. , vol.19 , pp. 4885-4894
    • Siniossoglou, S.1    Peak-Chew, S.Y.2    Pelham, H.R.3
  • 59
    • 0036701880 scopus 로고    scopus 로고
    • ARF1 regulatory factors and COPI vesicle formation
    • Spang, A. (2002). ARF1 regulatory factors and COPI vesicle formation. Curr. Opin. Cell Biol. 14, 423-427.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 423-427
    • Spang, A.1
  • 60
    • 0032530193 scopus 로고    scopus 로고
    • Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes
    • Spang, A., Matsuoka, K., Hamamoto, S., Schekman, R., and Orci, L. (1998). Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes. Proc. Natl. Acad. Sci. USA 95, 11199-11204.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11199-11204
    • Spang, A.1    Matsuoka, K.2    Hamamoto, S.3    Schekman, R.4    Orci, L.5
  • 61
    • 0033574678 scopus 로고    scopus 로고
    • A primer on vesicle budding
    • Springer, S., Spang, A., and Schekman, R. (1999). A primer on vesicle budding. Cell 97, 145-148.
    • (1999) Cell , vol.97 , pp. 145-148
    • Springer, S.1    Spang, A.2    Schekman, R.3
  • 62
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • Tanigawa, G., Orci, L., Amherdt, M., Ravazzola, M., Helms, J. B., and Rothman, J. E. (1993). Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123, 1365-1371.
    • (1993) J. Cell Biol. , vol.123 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5    Rothman, J.E.6
  • 63
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong, A. H., et al. (2001). Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294, 2364-2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.1
  • 64
    • 0141727533 scopus 로고    scopus 로고
    • Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling
    • Valdez-Taubas, J., and Pelham, H. R. (2003). Slow diffusion of proteins in the yeast plasma membrane allows polarity to be maintained by endocytic cycling. Curr. Biol. 13, 1636-1640.
    • (2003) Curr. Biol. , vol.13 , pp. 1636-1640
    • Valdez-Taubas, J.1    Pelham, H.R.2
  • 65
    • 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
    • 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.
    • (2002) Dev. Cell , vol.2 , pp. 283-294
    • Valdivia, R.H.1    Baggott, D.2    Chuang, J.S.3    Schekman, R.W.4
  • 66
    • 0028875216 scopus 로고
    • Cytoplasmic coat proteins involved in endosome function
    • Whitney, J. A., Gomez, M., Sheff, D., Kreis, T. E., and Mellman, I. (1995). Cytoplasmic coat proteins involved in endosome function. Cell 83, 703-713.
    • (1995) Cell , vol.83 , pp. 703-713
    • Whitney, J.A.1    Gomez, M.2    Sheff, D.3    Kreis, T.E.4    Mellman, I.5
  • 67
    • 0034678365 scopus 로고    scopus 로고
    • The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae
    • Wiederkehr, A., Avaro, S., Prescianotto-Baschong, C., Haguenauer-Tsapis, R., and Riezman, H. (2000). The F-box protein Rcy1p is involved in endocytic membrane traffic and recycling out of an early endosome in Saccharomyces cerevisiae. J. Cell Biol. 149, 397-410.
    • (2000) J. Cell Biol. , vol.149 , pp. 397-410
    • Wiederkehr, A.1    Avaro, S.2    Prescianotto-Baschong, C.3    Haguenauer-Tsapis, R.4    Riezman, H.5
  • 68
    • 0030050828 scopus 로고    scopus 로고
    • New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex
    • Wuestehube, L. J., Duden, R., Eun, A., Hamamoto, S., Korn, P., Ram, R., and Schekman, R. (1996). New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics 142, 393-406.
    • (1996) Genetics , vol.142 , pp. 393-406
    • Wuestehube, L.J.1    Duden, R.2    Eun, A.3    Hamamoto, S.4    Korn, P.5    Ram, R.6    Schekman, R.7
  • 69
    • 0037078331 scopus 로고    scopus 로고
    • ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat
    • Yang, J. S., Lee, S. Y., Gao, M., Bourgoin, S., Randazzo, P. A., Premont, R. T., and Hsu, V. W. (2002). ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J. Cell Biol. 159, 69-78.
    • (2002) J. Cell Biol. , vol.159 , pp. 69-78
    • Yang, J.S.1    Lee, S.Y.2    Gao, M.3    Bourgoin, S.4    Randazzo, P.A.5    Premont, R.T.6    Hsu, V.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.