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Volumn 135, Issue 3, 1996, Pages 585-595

Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMINO ACID; CHAPERONE; HISTIDINE; MEMBRANE PROTEIN; PERMEASE; PHEROMONE; SECRETORY PROTEIN;

EID: 0029831539     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.135.3.585     Document Type: Article
Times cited : (96)

References (59)
  • 1
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., L. Cao, and N. Kleckner. 1987. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics. 116:541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 2
    • 0027984387 scopus 로고
    • A family of vectors that facilitate transposon and insertional mutagenesis of cloned genes in yeast
    • Allen J.B., and S.J. Elledge. 1994. A family of vectors that facilitate transposon and insertional mutagenesis of cloned genes in yeast. Yeast. 10:1267-1272.
    • (1994) Yeast , vol.10 , pp. 1267-1272
    • Allen, J.B.1    Elledge, S.J.2
  • 3
    • 0029586511 scopus 로고
    • An overview of membrane transport proteins in Saccharomyces cerevisiae
    • Andre, B. 1995. An overview of membrane transport proteins in Saccharomyces cerevisiae. Yeast. 11:1575-1611.
    • (1995) Yeast , vol.11 , pp. 1575-1611
    • Andre, B.1
  • 4
    • 0027097849 scopus 로고
    • +2-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • +2-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell. 3:633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 5
    • 0024299523 scopus 로고
    • Reconstitution of SEC gene product-dependent intercompartmental protein transport
    • Baker, D., L. Hicke, M. Rexach, M. Schleyer, and R. Schekman. 1988. Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell. 54:335-344.
    • (1988) Cell , vol.54 , pp. 335-344
    • Baker, D.1    Hicke, L.2    Rexach, M.3    Schleyer, M.4    Schekman, R.5
  • 6
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E.K., N.J. Colley, and C.S. Zuker. 1994. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO (Eur. Mol. Biol. Organ.) J. 13:4886-4895.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 9
    • 0345109981 scopus 로고
    • A positive selection for mutants lacking orotidine 5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance
    • Boeke, J.D., F. Lacroute, and G.R. Fink. 1984. A positive selection for mutants lacking orotidine 5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance. Mol. Gen. Genet. 181:288-291.
    • (1984) Mol. Gen. Genet. , vol.181 , pp. 288-291
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 10
    • 0024024076 scopus 로고
    • Coincident localization of secretory and plasma membrane proteins in organelles of the yeast secretory pathway
    • Brada, D., and R. Schekman. 1988. Coincident localization of secretory and plasma membrane proteins in organelles of the yeast secretory pathway. J. Bacteriol. 170:2775-2783.
    • (1988) J. Bacteriol. , vol.170 , pp. 2775-2783
    • Brada, D.1    Schekman, R.2
  • 11
    • 0028988551 scopus 로고
    • 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein
    • Bu, G., H.J. Geuze, G.J. Strous, and A.L. Schwartz. 1995. 39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. EMBO (Eur. Mol. Biol. Organ.) J. 14:2269-2280.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 2269-2280
    • Bu, G.1    Geuze, H.J.2    Strous, G.J.3    Schwartz, A.L.4
  • 12
    • 0026039784 scopus 로고
    • Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport
    • Chang, A., and C.W. Slayman. 1991. Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport. J. Cell Biol. 115:289-295.
    • (1991) J. Cell Biol. , vol.115 , pp. 289-295
    • Chang, A.1    Slayman, C.W.2
  • 13
    • 0028795584 scopus 로고
    • Targeting of the yeast plasma membrane [H+]ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • Chang, A., and G.R. Fink. 1995. Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J. Cell Biol. 128:39-49.
    • (1995) J. Cell Biol. , vol.128 , pp. 39-49
    • Chang, A.1    Fink, G.R.2
  • 14
    • 0027961075 scopus 로고
    • The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway
    • Chapman, R.E., and S. Munro. 1994. The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANP1, a member of a new family of genes affecting the secretory pathway. EMBO (Eur. Mol. Biol. Organ.) J. 13: 4896-4907.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 4896-4907
    • Chapman, R.E.1    Munro, S.2
  • 15
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N.J., E.K. Baker, M.A. Stamnes, and C.S. Zuker. 1991. The cyclophilin homolog ninaA is required in the secretory pathway. Cell. 67:255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 16
    • 0020539159 scopus 로고
    • Ammonia regulation of amino acid permeases in Saccharomyces cerevisiae
    • Courchesne, W.E., and B. Magasanik. 1983. Ammonia regulation of amino acid permeases in Saccharomyces cerevisiae. Mol. Cell. Biol. 3:672-683.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 672-683
    • Courchesne, W.E.1    Magasanik, B.2
  • 17
    • 0028838294 scopus 로고
    • Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene
    • de Kerchove d'Exaerde, A., P. Supply, J.P. Dufour, P. Bogaerts, D. Thines, A. Goffeau, and M. Boutry. 1995. Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene. J. Biol. Chem. 270:23828-23837.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23828-23837
    • De Kerchove D'Exaerde, A.1    Supply, P.2    Dufour, J.P.3    Bogaerts, P.4    Thines, D.5    Goffeau, A.6    Boutry, M.7
  • 18
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles
    • Doering, T.L., and R. Schekman. 1996. GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles. EMBO (Eur. Mol. Biol. Organ.) J. 15:182-191.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 19
    • 0028803617 scopus 로고
    • Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p
    • Espenshade, P., R.E. Gimeno, E. Holzmacher, P. Teung, and C.A. Kaiser. 1995. Yeast SEC16 gene encodes a multidomain vesicle coat protein that interacts with Sec23p. J. Cell Biol. 131:311-324.
    • (1995) J. Cell Biol. , vol.131 , pp. 311-324
    • Espenshade, P.1    Gimeno, R.E.2    Holzmacher, E.3    Teung, P.4    Kaiser, C.A.5
  • 20
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G.I., G.K. Lewis, G. Ramsay, and J.M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 21
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J., and J. Sambrook. 1992. Protein folding in the cell. Nature (Lond.). 355:33-45.
    • (1992) Nature (Lond.) , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 22
    • 0026531641 scopus 로고
    • Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae
    • Green, N., H. Fang, and P. Walter. 1992. Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J. Cell Biol. 116:597-604.
    • (1992) J. Cell Biol. , vol.116 , pp. 597-604
    • Green, N.1    Fang, H.2    Walter, P.3
  • 23
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C., and G.R. Fink. 1991. Guide to yeast genetics and molecular biology. Methods Enzymol. 194:186-187.
    • (1991) Methods Enzymol. , vol.194 , pp. 186-187
    • Guthrie, C.1    Fink, G.R.2
  • 24
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 1995. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7:523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 26
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E., and A. Bretscher. 1995. Parallel secretory pathways to the cell surface in yeast. J. Cell Biol. 131:297-310.
    • (1995) J. Cell Biol. , vol.131 , pp. 297-310
    • Harsay, E.1    Bretscher, A.2
  • 27
    • 0028109216 scopus 로고
    • Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex
    • Hill, K.J., and T.H. Stevens. 1994. Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H(+)-ATPase complex. Mol. Biol. Cell. 5: 1039-1050.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1039-1050
    • Hill, K.J.1    Stevens, T.H.2
  • 28
    • 0027439523 scopus 로고
    • VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae
    • Hirata, R., N. Umemoto, M.N. Ho, Y. Ohya, T.H. Stevens, and Y. Anraku. 1993. VMA12 is essential for assembly of the vacuolar H(+)-ATPase subunits onto the vacuolar membrane in Saccharomyces cerevisiae. J. Biol. Chem. 268:961-967.
    • (1993) J. Biol. Chem. , vol.268 , pp. 961-967
    • Hirata, R.1    Umemoto, N.2    Ho, M.N.3    Ohya, Y.4    Stevens, T.H.5    Anraku, Y.6
  • 29
    • 0023853298 scopus 로고
    • Secretory vesicles externalize the major plasma membrane ATPase in yeast
    • Holcomb, C.L., W.J. Hansen, T. Etcheverry, and R. Schekman. 1988. Secretory vesicles externalize the major plasma membrane ATPase in yeast. J. Cell Biol. 106:641-648.
    • (1988) J. Cell Biol. , vol.106 , pp. 641-648
    • Holcomb, C.L.1    Hansen, W.J.2    Etcheverry, T.3    Schekman, R.4
  • 30
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej, P.A. and R.A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 31
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D. Roberts and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154: 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 32
    • 0027241227 scopus 로고
    • Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence
    • Lian, J.P., and S. Ferro-Novick. 1993. Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence. Cell. 73:735-745.
    • (1993) Cell , vol.73 , pp. 735-745
    • Lian, J.P.1    Ferro-Novick, S.2
  • 33
    • 0026446549 scopus 로고
    • SHR3: A novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast
    • Ljungdahl, P.O., C.J. Gimeno, C.A. Styles, and G.R. Fink. 1992. SHR3: a novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast. Cell. 71:463-478.
    • (1992) Cell , vol.71 , pp. 463-478
    • Ljungdahl, P.O.1    Gimeno, C.J.2    Styles, C.A.3    Fink, G.R.4
  • 34
    • 0023615620 scopus 로고
    • Plasmid construction by homologous recombination in yeast
    • Ma, H., S. Kunes, P.J. Schatz, and D. Botstein. 1987. Plasmid construction by homologous recombination in yeast. Gene (Amst.). 58:201-216.
    • (1987) Gene (Amst.) , vol.58 , pp. 201-216
    • Ma, H.1    Kunes, S.2    Schatz, P.J.3    Botstein, D.4
  • 35
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade, G. 1975. Intracellular aspects of the process of protein secretion. Science (Wash. DC). 189:347-358.
    • (1975) Science (Wash. DC) , vol.189 , pp. 347-358
    • Palade, G.1
  • 37
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach, M., and R.W. Schekman. 1991. Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles. J. Cell Biol. 114:219-229.
    • (1991) J. Cell Biol. , vol.114 , pp. 219-229
    • Rexach, M.1    Schekman, R.W.2
  • 38
    • 0027965738 scopus 로고
    • Characteristics of endoplasmic reticulum-derived transport vesicles
    • Rexach, M.F., M. Latterich, and R. Schekman. 1994. Characteristics of endoplasmic reticulum-derived transport vesicles. J. Cell Biol. 126:1133-1148.
    • (1994) J. Cell Biol. , vol.126 , pp. 1133-1148
    • Rexach, M.F.1    Latterich, M.2    Schekman, R.3
  • 39
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J.E. 1994. Mechanisms of intracellular protein transport. Nature (Lond.). 372:55-63.
    • (1994) Nature (Lond.) , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 40
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • Salama, N.R., T. Yeung, and R.W. Schekman. 1993. The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO (Eur. Mol. Biol. Organ.) J. 12:4073-4082.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 41
    • 0023140642 scopus 로고
    • Secretory pattern of a major integral mannoprotein of the yeast cell wall
    • Sanz, P., E. Herrero, and R. Sentandreu. 1987. Secretory pattern of a major integral mannoprotein of the yeast cell wall. Biochim. Biophys. Acta. 924:193-203.
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 193-203
    • Sanz, P.1    Herrero, E.2    Sentandreu, R.3
  • 42
    • 0026908303 scopus 로고
    • Genetic and biochemical analysis of vesicular traffic in yeast
    • Schekman, R. 1992. Genetic and biochemical analysis of vesicular traffic in yeast. Curr. Opin. Cell Biol. 4:587-592.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 587-592
    • Schekman, R.1
  • 43
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and L. Orci. 1996. Coat proteins and vesicle budding. Science (Wash. DC). 271:1526-1533.
    • (1996) Science (Wash. DC) , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 44
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmoller, F., B. Singer-Kruger, S. Schroder, U. Kruger, C. Barlowe, and H. Riezman. 1995. The absence of Emp24p, a component of ER derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO (Eur. Mol. Biol. Oragn.) J. 14:1329-1339.
    • (1995) EMBO (Eur. Mol. Biol. Oragn.) J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 45
    • 0027959012 scopus 로고
    • Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake
    • Schmidt, A., M.N. Hall, and A. Koller. 1994. Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake. Mol. Cell. Biol. 14:6597-6606.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6597-6606
    • Schmidt, A.1    Hall, M.N.2    Koller, A.3
  • 48
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 49
    • 0028867027 scopus 로고
    • Mutation of RGA1, which encodes a putative GTPase-activating protein for polarity-establishment protein Cdc42p, activates the pheromone-response pathway in the yeast Saccharomyces cerevisiae
    • Stevenson, B.J., B. Ferguson, C. De Virgilio, E. Bi, J.R. Pringle, G. Ammerer, and G.F. Sprague Jr. 1995. Mutation of RGA1, which encodes a putative GTPase-activating protein for polarity-establishment protein Cdc42p, activates the pheromone-response pathway in the yeast Saccharomyces cerevisiae. Genes Dev. 9:2949-2963.
    • (1995) Genes Dev. , vol.9 , pp. 2949-2963
    • Stevenson, B.J.1    Ferguson, B.2    De Virgilio, C.3    Bi, E.4    Pringle, J.R.5    Ammerer, G.6    Sprague Jr., G.F.7
  • 50
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C.J., J. Rothblatt, M. Hosobuchi, R. Deshaies, and R. Schekman. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell. 3:129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 51
    • 0025201631 scopus 로고
    • The ADE2 gene from Saccharomyces cerevisiae: Sequence and new vectors
    • Stotz, A. and P. Linder. 1990. The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors. Gene (Amst.). 95:91-98.
    • (1990) Gene (Amst.) , vol.95 , pp. 91-98
    • Stotz, A.1    Linder, P.2
  • 52
    • 0022340382 scopus 로고
    • The histidine permease gene (HIPI) of Saccharomyces cerevisiae
    • Tanaka, J., and G.R. Fink. 1985. The histidine permease gene (HIPI) of Saccharomyces cerevisiae. Gene (Amst.). 38:205-214.
    • (1985) Gene (Amst.) , vol.38 , pp. 205-214
    • Tanaka, J.1    Fink, G.R.2
  • 53
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J., and J. Messing. 1987. Production of single-stranded plasmid DNA. Methods Enzymol. 153:3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 54
    • 0026653810 scopus 로고
    • Functional expression of plant plasma membrane H(+)-ATPase in yeast endoplasmic reticulum
    • Villalba, J.M., M.G. Palmgren, G.E. Berberian, C. Ferguson, and R. Serrano. 1992. Functional expression of plant plasma membrane H(+)-ATPase in yeast endoplasmic reticulum. J. Biol. Chem. 267:12341-12349.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12341-12349
    • Villalba, J.M.1    Palmgren, M.G.2    Berberian, G.E.3    Ferguson, C.4    Serrano, R.5
  • 55
    • 0023368570 scopus 로고
    • Purification and characterization of constitutive secretory vesicles from yeast
    • Walworth, N.C., and P.J. Novick. 1987. Purification and characterization of constitutive secretory vesicles from yeast. J. Cell Biol. 105:163-174.
    • (1987) J. Cell Biol. , vol.105 , pp. 163-174
    • Walworth, N.C.1    Novick, P.J.2
  • 57
    • 0027015925 scopus 로고
    • Reconstitution of transport from the endoplasmic reticulum to the Golgi complex using an ER-enriched membrane fraction from yeast
    • Wuestehube, L.J., and R. Schekman. 1992. Reconstitution of transport from the endoplasmic reticulum to the Golgi complex using an ER-enriched membrane fraction from yeast. Methods Enzymol. 219:124-136.
    • (1992) Methods Enzymol. , vol.219 , pp. 124-136
    • Wuestehube, L.J.1    Schekman, R.2
  • 58
    • 0029587314 scopus 로고
    • Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum
    • Yeung, T., C. Barlowe, and R. Schekman. 1995. Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum. J. Biol. Chem. 270:30567-30570.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30567-30570
    • Yeung, T.1    Barlowe, C.2    Schekman, R.3
  • 59
    • 0029808478 scopus 로고    scopus 로고
    • Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway
    • In press
    • Ziman, M., J. Chuang, and R. Schekman. 1996. Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway. Mol. Biol. Cell. In press.
    • (1996) Mol. Biol. Cell
    • Ziman, M.1    Chuang, J.2    Schekman, R.3


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