메뉴 건너뛰기




Volumn 171, Issue 5, 2005, Pages 823-833

Mutants in trs 120 disrupt traffic from the early endosome to the late Golgi

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEIN SUBUNIT; COAT PROTEIN COMPLEX I; GUANINE NUCLEOTIDE EXCHANGE FACTOR; MEMBRANE PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SEC7 GUANINE NUCLEOTIDE EXCHANGE FACTORS; TRANSPORT PROTEIN PARTICLE, TRAPP; TRS130 PROTEIN, S CEREVISIAE; VESICULAR TRANSPORT PROTEIN;

EID: 28544431984     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200505145     Document Type: Article
Times cited : (103)

References (60)
  • 1
    • 0029869843 scopus 로고    scopus 로고
    • An endosomal βCOP is involved in the pH-dependent formation of transport vesicles destined for late endosomes
    • Aniento, F., F. Gu, R. Parton, and J. Gruenberg. 1996. An endosomal βCOP 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.3    Gruenberg, J.4
  • 2
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T.K. Sato, L.M. Banta, and S.D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831.
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 3
    • 0000272957 scopus 로고
    • Isolation of yeast mutants defective in protein targeting to the vacuole
    • Bankaitis, V.A., L.M. Johnson, and S.D. Emr. 1986. Isolation of yeast mutants defective in protein targeting to the vacuole. Proc. Natl. Acad. Sci. USA. 83:9075-9079.
    • (1986) Proc. Natl. Acad. Sci. USA. , vol.83 , pp. 9075-9079
    • Bankaitis, V.A.1    Johnson, L.M.2    Emr, S.D.3
  • 5
    • 0034161259 scopus 로고    scopus 로고
    • TRAPP stably associates with the Golgi and is required for vesicle docking
    • Barrowman, J., M. Sacher, and S. Ferro-Novick. 2000. TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J. 19:862-869.
    • (2000) EMBO J. , vol.19 , pp. 862-869
    • Barrowman, J.1    Sacher, M.2    Ferro-Novick, S.3
  • 6
    • 0029804680 scopus 로고    scopus 로고
    • Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast
    • Benli, M., F. Doring, D.G. Robinson, X. Yang, and D. Gallwitz. 1996. Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function in yeast. EMBO J. 15:6460-6475.
    • (1996) EMBO J. , vol.15 , pp. 6460-6475
    • Benli, M.1    Doring, F.2    Robinson, D.G.3    Yang, X.4    Gallwitz, D.5
  • 7
    • 0033984895 scopus 로고    scopus 로고
    • Organization of the yeast Golgi complex into at least four functionally distinct compartments
    • Brigance, W.T., C. Barlowe, and T.R. Graham. 2000. Organization of the yeast Golgi complex into at least four functionally distinct compartments. Mol. Biol. Cell. 11:171-182.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 171-182
    • Brigance, W.T.1    Barlowe, C.2    Graham, T.R.3
  • 8
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol (3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • Burd, C.G., and S.D. Emr. 1998. Phosphatidylinositol (3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell. 2:157-162.
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 9
    • 0033552605 scopus 로고    scopus 로고
    • Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function
    • Chen, C.Y., M.F. Ingram, P.H. Rosal, and T.R. Graham. 1999. Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J. Cell Biol. 147:1223-1236.
    • (1999) J. Cell Biol. , vol.147 , pp. 1223-1236
    • Chen, C.Y.1    Ingram, M.F.2    Rosal, P.H.3    Graham, T.R.4
  • 10
    • 0029844403 scopus 로고    scopus 로고
    • Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p
    • Chuang, J., and R. Schekman. 1996. Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p. J. Cell Biol. 135:597-610.
    • (1996) J. Cell Biol. , vol.135 , pp. 597-610
    • Chuang, J.1    Schekman, R.2
  • 11
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • Conibear, E., J.N. Cleck, and T.H. Stevens. 2003. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol. Biol. Cell. 14:1610-1623.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 12
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper, A.A., and T.H. Stevens. 1996. Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J. Cell Biol. 133:529-541.
    • (1996) J. Cell Biol. , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 13
    • 0031425955 scopus 로고    scopus 로고
    • Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component ε-COP
    • Daro, E., D. Sheff, M. Gomez, T. Kreis, and I. Mellman. 1997. Inhibition of endosome function in CHO cells bearing a temperature-sensitive defect in the coatomer (COPI) component ε-COP. J. Cell Biol. 139:1747-1759.
    • (1997) J. Cell Biol. , vol.139 , pp. 1747-1759
    • Daro, E.1    Sheff, D.2    Gomez, M.3    Kreis, T.4    Mellman, I.5
  • 14
    • 0027175829 scopus 로고
    • Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors
    • Davis, N.G., J.L. Horecka, and G.F. Sprague Jr. 1993. Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors. J. Cell Biol. 122:53-65.
    • (1993) J. Cell Biol. , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sprague Jr., G.F.3
  • 16
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., K. Redding, J. Crosby, R.S. Fuller, and R. Schekman. 1991. Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 112:27-37.
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 17
    • 0023838558 scopus 로고
    • Enzymes required for yeast prohormone processing
    • Fuller, R.S., R.E. Sterne, and J. Thorner. 1988. Enzymes required for yeast prohormone processing. Annu. Rev. Physiol. 50:345-362.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 345-362
    • Fuller, R.S.1    Sterne, R.E.2    Thorner, J.3
  • 20
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T.R., and S.D. Emr. 1991. Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114:207-218.
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 22
    • 0037148531 scopus 로고    scopus 로고
    • A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway
    • Harsay, E., and R. Schekman. 2002. A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J. Cell Biol. 156:271-285.
    • (2002) J. Cell Biol. , vol.156 , pp. 271-285
    • Harsay, E.1    Schekman, R.2
  • 23
    • 0030803426 scopus 로고    scopus 로고
    • Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein
    • Hicke, L., B. Zanolari, M. Pypaert, J. Rohrer, and H. Riezman. 1997. Transport through the yeast endocytic pathway occurs through morphologically distinct compartments and requires an active secretory pathway and Sec18p/N-ethylmaleimide-sensitive fusion protein. Mol. Biol. Cell. 8:13-31.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 13-31
    • Hicke, L.1    Zanolari, B.2    Pypaert, M.3    Rohrer, J.4    Riezman, H.5
  • 24
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis, J.C., B.J. Nichols, S. Dhruvakumar, and H.R. Pelham. 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
  • 25
    • 0026620198 scopus 로고
    • SEC21 is a gene required for ER to Golgi protein transport that encodes a subunit of a yeast coatomer
    • Hosobuchi, M., T. Kreis, and R. Schekman. 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
  • 26
    • 0030969912 scopus 로고    scopus 로고
    • Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment
    • Jedd, G., J. Mulholland, and N. Segev. 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
  • 27
    • 0033638091 scopus 로고    scopus 로고
    • The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32
    • Jones, S., C. Newman, F. Liu, and N. Segev. 2000. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol. Biol. Cell. 11:4403-4411.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4403-4411
    • Jones, S.1    Newman, C.2    Liu, F.3    Segev, N.4
  • 28
    • 0042991262 scopus 로고    scopus 로고
    • Vps27 recruits ESCRT machinery to endosomes during MVB sorting
    • Katzmann, D.J., C.J. Stefan, M. Babst, and S.D. Emr. 2003. Vps27 recruits ESCRT machinery to endosomes during MVB sorting. J. Cell Biol. 162:413-423.
    • (2003) J. Cell Biol. , vol.162 , pp. 413-423
    • Katzmann, D.J.1    Stefan, C.J.2    Babst, M.3    Emr, S.D.4
  • 31
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 32
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E.G., B.F. Horazdovsky, J.L. Cereghino, E. Gharakhanian, and S.D. Emr. 1994. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene. Cell. 77:579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 33
    • 0026749963 scopus 로고
    • OCH1 encodes a novel membrane bound mannosyltransferase: Outer chain elongation of asparagine-linked oligosaccharides
    • Nakayama, K., T. Nagasu, Y. Shimma, J. Kuromitsu, and Y. Jigami. 1992. OCH1 encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine-linked oligosaccharides. EMBO J. 11:2511-2519.
    • (1992) EMBO J. , vol.11 , pp. 2511-2519
    • Nakayama, K.1    Nagasu, T.2    Shimma, Y.3    Kuromitsu, J.4    Jigami, Y.5
  • 35
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Nothwehr, S.F., C.J. Roberts, and T.H. Stevens. 1993. Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J. Cell Biol. 121:1197-1209.
    • (1993) J. Cell Biol. , vol.121 , pp. 1197-1209
    • Nothwehr, S.F.1    Roberts, C.J.2    Stevens, T.H.3
  • 36
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., C. Field, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 21:205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 37
    • 0028800173 scopus 로고
    • VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae
    • Piper, R.C., A.A. Cooper, H. Yang, and T.H. Stevens. 1995. VPS27 controls vacuolar and endocytic traffic through a prevacuolar compartment in Saccharomyces cerevisiae. J. Cell Biol. 131:603-617.
    • (1995) J. Cell Biol. , vol.131 , pp. 603-617
    • Piper, R.C.1    Cooper, A.A.2    Yang, H.3    Stevens, T.H.4
  • 39
    • 0027249359 scopus 로고
    • Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae
    • Protopopov, V., B. Govindan, P. Novick, and J.E. Gerst. 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
  • 40
    • 0027199241 scopus 로고
    • Yeast endocytosis
    • Riezman, H. 1993. Yeast endocytosis. Trends Cell Biol. 3:273-277.
    • (1993) Trends Cell Biol. , vol.3 , pp. 273-277
    • Riezman, H.1
  • 42
    • 0028864441 scopus 로고
    • BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs
    • Rossi, G., K. Kolstad, S. Stone, F. Palluault, and S. Ferro-Novick. 1995. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Mol. Biol. Cell. 6:1769-1780.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1769-1780
    • Rossi, G.1    Kolstad, K.2    Stone, S.3    Palluault, F.4    Ferro-Novick, S.5
  • 43
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J.E., and F.T. Wieland. 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
  • 44
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • Rothman, J.H., and T.H. Stevens. 1986. Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell. 47:1041-1051.
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 46
    • 12844258045 scopus 로고    scopus 로고
    • Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies components in a Golgi-specific Ypt31/rab-GTPase signaling pathway
    • Sciorra, V.A., A. Audhya, A.B. Parsons, N. Segev, C. Boone, and S.D. Emr. 2005. Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies components in a Golgi-specific Ypt31/rab-GTPase signaling pathway. Mol. Biol. Cell. 16:776-793.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 776-793
    • Sciorra, V.A.1    Audhya, A.2    Parsons, A.B.3    Segev, N.4    Boone, C.5    Emr, S.D.6
  • 47
    • 0027312380 scopus 로고
    • Partial purification and characterization of early and late endosomes from yeast. Identification of four novel proteins
    • Singer-Kruger, B., R. Frank, F. Crausaz, and H. Riezman. 1993. Partial purification and characterization of early and late endosomes from yeast. Identification of four novel proteins. J. Biol. Chem. 268:14376-14386.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14376-14386
    • Singer-Kruger, B.1    Frank, R.2    Crausaz, F.3    Riezman, H.4
  • 48
    • 0032734240 scopus 로고    scopus 로고
    • The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton
    • Spelbrink, R.G., and S.F. Nothwehr. 1999. The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton. Mol. Biol. Cell. 10:4263-4281.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4263-4281
    • Spelbrink, R.G.1    Nothwehr, S.F.2
  • 49
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T., B. Esmon, and R. Schekman. 1982. Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole. Cell. 30:439-448.
    • (1982) Cell , vol.30 , pp. 439-448
    • Stevens, T.1    Esmon, B.2    Schekman, R.3
  • 50
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34p/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • Suvorova, E.S., R. Duden, and V.V. Lupashin. 2002. The Sec34p/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J. Cell Biol. 157:631-643.
    • (2002) J. Cell Biol. , vol.157 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 51
    • 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., D. Baggott, J.S. Chuang, and R.W. Schekman. 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
  • 52
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and S.D. Emr. 1995. A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J. Cell Biol. 128:779-792.
    • (1995) J. Cell Biol. , vol.128 , pp. 779-792
    • Vida, T.A.1    Emr, S.D.2
  • 53
    • 0027297956 scopus 로고
    • Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment
    • Vida, T.A., G. Huyer, and S.D. Emr. 1993. Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment. J. Cell Biol. 121:1245-1256.
    • (1993) J. Cell Biol. , vol.121 , pp. 1245-1256
    • Vida, T.A.1    Huyer, G.2    Emr, S.D.3
  • 54
    • 0036736141 scopus 로고    scopus 로고
    • A Ypt32p exchange factor is a putative effector of Ypt1p
    • Wang, W., and S. Ferro-Novick. 2002. A Ypt32p exchange factor is a putative effector of Ypt1p. Mol. Biol. Cell. 13:3336-3343.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 3336-3343
    • Wang, W.1    Ferro-Novick, S.2
  • 55
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte, J.R., and S. Munro. 2001. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev. Cell. 1:527-537.
    • (2001) Dev. Cell. , vol.1 , pp. 527-537
    • Whyte, J.R.1    Munro, S.2
  • 56
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte, J.R., and S. Munro. 2002. Vesicle tethering complexes in membrane traffic. J. Cell Sci. 115:2627-2637.
    • (2002) J. Cell Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 57
    • 0027080272 scopus 로고
    • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole
    • Wilcox, C.A., K. Redding, R. Wright, and R.S. Fuller. 1992. Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol. Biol. Cell. 3:1353-1371.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1353-1371
    • Wilcox, C.A.1    Redding, K.2    Wright, R.3    Fuller, R.S.4
  • 58
    • 0036872206 scopus 로고    scopus 로고
    • Mutation of TRS130, which encodes a component of the TRAPP II complex, activates transcription of OCH1 in Saccharomyces cerevisiae
    • Yamamoto, K., and Y. Jigami. 2002. Mutation of TRS130, which encodes a component of the TRAPP II complex, activates transcription of OCH1 in Saccharomyces cerevisiae. Curr. Genet. 42:85-93.
    • (2002) Curr. Genet. , vol.42 , pp. 85-93
    • Yamamoto, K.1    Jigami, Y.2
  • 60
    • 14744272136 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • Zolov, S.N., and V.V. Lupashin. 2005. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J. Cell Biol. 168:747-759.
    • (2005) J. Cell Biol. , vol.168 , pp. 747-759
    • Zolov, S.N.1    Lupashin, V.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.