메뉴 건너뛰기




Volumn 139, Issue 1, 1997, Pages 23-36

SOI1 encodes a novel, conserved protein that promotes TGN-endosomal cycling of Kex2p and other membrane proteins by modulating the function of two TGN localization signals

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; MEMBRANE PROTEIN; PROTEINASE;

EID: 0030762073     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.1.23     Document Type: Article
Times cited : (155)

References (55)
  • 2
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 4
    • 0001156518 scopus 로고
    • One-step site-directed mutagenesis of the Kex2 protease oxyanion hole
    • Brenner, C., A. Bevan, and R.S. Fuller. 1993. One-step site-directed mutagenesis of the Kex2 protease oxyanion hole. Curr. Biol. 3:498-506.
    • (1993) Curr. Biol. , vol.3 , pp. 498-506
    • Brenner, C.1    Bevan, A.2    Fuller, R.S.3
  • 5
    • 0031055434 scopus 로고    scopus 로고
    • Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention
    • Bryant, N.J., and T.H. Stevens. 1997. Two separate signals act independently to localize a yeast late Golgi membrane protein through a combination of retrieval and retention. J. Cell Biol. 136:287-297.
    • (1997) J. Cell Biol. , vol.136 , pp. 287-297
    • Bryant, N.J.1    Stevens, T.H.2
  • 6
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization
    • Cereghino, J.L., E.G. Marcusson, and S.D. Emr. 1995. The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localization. Mol. Biol. Cell. 6:1089-1102.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 7
    • 0028283375 scopus 로고
    • Retrieval of TGN proteins from the cell surface requires endosomal acidification
    • Chapman, R.E., and S. Munro. 1994. Retrieval of TGN proteins from the cell surface requires endosomal acidification. EMBO (Eur. Mol. Biol. Organ.) J. 13:2305-2312.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 2305-2312
    • Chapman, R.E.1    Munro, S.2
  • 8
    • 0027085824 scopus 로고
    • Yeast Kex1p is a Golgi-associated membrane protein: Deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane
    • Cooper, A., and H. Bussey. 1992. Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane. J. Cell Biol. 119:1459-1468.
    • (1992) J. Cell Biol. , vol.119 , pp. 1459-1468
    • Cooper, A.1    Bussey, H.2
  • 9
    • 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
  • 10
    • 0016748609 scopus 로고
    • Polybase-induced lysis of yeast spheroplasts
    • Durr, M., T. Boller, and A. Wiemken. 1975. Polybase-induced lysis of yeast spheroplasts. Arch. Microbiol. 105:319-327.
    • (1975) Arch. Microbiol. , vol.105 , pp. 319-327
    • Durr, M.1    Boller, T.2    Wiemken, A.3
  • 11
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson, M.J., and C.A. Kaiser. 1996. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol. Biol. Cell. 7:1043-1058.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 12
    • 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
  • 13
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function and disease
    • Fuchs, E., and K. Weber. 1994. Intermediate filaments: structure, dynamics, function and disease. Annu. Rev. Biochem. 63:345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hofmann, K., and W. Stoffel. 1993. TMbase - a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler. 347:166.
    • (1993) Biol. Chem. Hoppe-Seyler. , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 18
    • 0017600514 scopus 로고
    • Proteinase mutants of Saccharomyces cerevisiae
    • Jones, E.W. 1977. Proteinase mutants of Saccharomyces cerevisiae. Genetics. 85:23-33.
    • (1977) Genetics , vol.85 , pp. 23-33
    • Jones, E.W.1
  • 19
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor
    • Julius, D., A. Brake, L. Blair, R. Kunisawa, and J. Thorner. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-alpha-factor. Cell. 37:1075-1089.
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 20
    • 0024006019 scopus 로고
    • Intracellular sorting and processing of a yeast vacuolar hydrolase: Proteinase A propeptide contains vacuolar targeting information
    • Klionsky, D.J., L.M. Banta, and S.D. Emr. 1988. Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. Mol. Cell. Biol. 8:2105-2116.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2105-2116
    • Klionsky, D.J.1    Banta, L.M.2    Emr, S.D.3
  • 21
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionsky, D.J., and S.D. Emr. 1989. Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO (Eur. Mol. Biol. Organ.) J. 8:2241-2250.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 2241-2250
    • Klionsky, D.J.1    Emr, S.D.2
  • 22
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors
    • Kornfeld, S. 1992. Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors. Annu. Rev. Biochem. 61:307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 23
    • 0029831539 scopus 로고    scopus 로고
    • Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro
    • Kuehn, M.J., R. Schekman, and P.O. Ljungdahl. 1996. Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J. Cell Biol. 135: 585-595.
    • (1996) J. Cell Biol. , vol.135 , pp. 585-595
    • Kuehn, M.J.1    Schekman, R.2    Ljungdahl, P.O.3
  • 24
    • 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. 100:367-382.
    • (1987) Methods Enzymol. , vol.100 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 25
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas, A. 1996. Prediction and analysis of coiled-coil structures. Methods Enzymol. 266:513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 26
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science (Wash. DC). 252:1162-1164.
    • (1991) Science (Wash. DC) , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 27
    • 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
  • 28
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane
    • Nothwehr, S.F., E. Conibear, and T.H. Stevens. 1995. Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane. J. Cell Biol. 129:35-46.
    • (1995) J. Cell Biol. , vol.129 , pp. 35-46
    • Nothwehr, S.F.1    Conibear, E.2    Stevens, T.H.3
  • 29
    • 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
  • 30
    • 0028283489 scopus 로고
    • Sorting of membrane proteins in the yeast secretory pathway
    • Nothwehr, S.F., and T.H. Stevens. 1994. Sorting of membrane proteins in the yeast secretory pathway. J. Biol. Chem. 269:10185-10188.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10185-10188
    • Nothwehr, S.F.1    Stevens, T.H.2
  • 31
    • 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
  • 32
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond, C.K., S.I. Howald, C.A. Vater, and T.H. Stevens. 1992. Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol. Biol. Cell. 3:1389-1402.
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howald, S.I.2    Vater, C.A.3    Stevens, T.H.4
  • 33
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J.C., and H.R.B. Pelham. 1997. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO (Eur. Mol. Biol. Organ.) J. 16:1832-1841.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.B.2
  • 34
    • 0029833575 scopus 로고    scopus 로고
    • Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins
    • Redding, K., J.H. Brickner, L.G. Marschall, J.W. Nichols, and R.S. Fuller. 1996. Allele-specific suppression of a defective trans-Golgi network (TGN) localization signal in Kex2p identifies three genes involved in localization of TGN transmembrane proteins. Mol. Cell. Biol. 16:6208-6217.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6208-6217
    • Redding, K.1    Brickner, J.H.2    Marschall, L.G.3    Nichols, J.W.4    Fuller, R.S.5
  • 35
    • 0025752784 scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding, K., C. Holcomb, and R.S. Fuller. 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell Biol. 113:527-538.
    • (1991) J. Cell Biol. , vol.113 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 36
    • 0029905944 scopus 로고    scopus 로고
    • The effects of clathrin inactivation on localization of Kex2 protease are independent of the TGN localization signal in the cytosolic tail of Kex2p
    • Redding, K.E., M. Seeger, G.S. Payne, and R.S. Fuller. 1996. The effects of clathrin inactivation on localization of Kex2 protease are independent of the TGN localization signal in the cytosolic tail of Kex2p. Mol. Biol. Cell. 7:1667-1677.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 1667-1677
    • Redding, K.E.1    Seeger, M.2    Payne, G.S.3    Fuller, R.S.4
  • 37
    • 0029954332 scopus 로고    scopus 로고
    • Multilamellar endosome-like compartment acculumates in the yeast vps28 vacuolar protein sorting mutant
    • Rieder, S.E., L.M. Banta, K. Koher, J.M. McCaffery, and S.D. Emr. 1996. Multilamellar endosome-like compartment acculumates in the yeast vps28 vacuolar protein sorting mutant. Mol. Biol. Cell. 7:985-999.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 985-999
    • Rieder, S.E.1    Banta, L.M.2    Koher, K.3    McCaffery, J.M.4    Emr, S.D.5
  • 40
    • 0022470653 scopus 로고
    • Overproduction-induced mislocalization of a yeast vacuolar protein allows isolation of its structural gene
    • Rothman, J.H., C.P. Hunter, L.A. Valls, and T.H. Stevens. 1986. Overproduction-induced mislocalization of a yeast vacuolar protein allows isolation of its structural gene. Proc. Natl. Acad. Sci. USA. 83:3248-3252.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3248-3252
    • Rothman, J.H.1    Hunter, C.P.2    Valls, L.A.3    Stevens, T.H.4
  • 41
    • 0025376380 scopus 로고
    • A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting
    • Rothman, J.H., C.K. Raymond, T. Gilbert, P.J. O'Hara, and T.H. Stevens. 1990. A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting. Cell. 61:1063-1074.
    • (1990) Cell , vol.61 , pp. 1063-1074
    • Rothman, J.H.1    Raymond, C.K.2    Gilbert, T.3    O'Hara, P.J.4    Stevens, T.H.5
  • 42
    • 0004136246 scopus 로고
    • C. Nolan, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., E.F. Fritsch, and T. Maniatis. 1989. Molecular Cloning. C. Nolan, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 43
    • 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. Schröder, 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. Organ.) J. 14:1329-1339.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schröder, S.3    Kruger, U.4    Barlowe, C.5    Riezman, H.6
  • 44
    • 0026652588 scopus 로고
    • A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast
    • Seeger, M., and G.S. Payne. 1992. A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast. EMBO (Eur. Mol. Biol. Organ.) J. 11:2811-2818.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 2811-2818
    • Seeger, M.1    Payne, G.S.2
  • 45
    • 0026742306 scopus 로고
    • Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae
    • Seeger, M., and G.S. Payne. 1992. Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae. J. Cell Biol. 118:531-540.
    • (1992) J. Cell Biol. , vol.118 , pp. 531-540
    • Seeger, M.1    Payne, G.S.2
  • 46
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Silkorsky, 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
    • Silkorsky, R.S.1    Hieter, P.2
  • 47
    • 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
  • 48
    • 0028875689 scopus 로고
    • Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain
    • Takahashi, S., T. Nakagawa, T. Banno, T. Watanabe, K. Murakami, and K. Nakayama. 1995. Localization of furin to the trans-Golgi network and recycling from the cell surface involves Ser and Tyr residues within the cytoplasmic domain. J. Biol. Chem. 270:28397-28401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28397-28401
    • Takahashi, S.1    Nakagawa, T.2    Banno, T.3    Watanabe, T.4    Murakami, K.5    Nakayama, K.6
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., D.G. Higgins, and T.J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 50
    • 0026509543 scopus 로고
    • The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation
    • Tyers, M., G. Tokiwa, R. Nash, and B. Futcher. 1992. The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation. EMBO (Eur. Mol. Biol. Organ.) J. 11:1773-1784 .
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 1773-1784
    • Tyers, M.1    Tokiwa, G.2    Nash, R.3    Futcher, B.4
  • 51
    • 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
  • 52
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast. 10:3793-1808.
    • (1994) Yeast , vol.10 , pp. 3793-11808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 53
    • 0024999340 scopus 로고
    • Single-step purification of shuttle vectors from yeast for high frequency back-transformation into E. coli
    • Ward, A.C. 1990. Single-step purification of shuttle vectors from yeast for high frequency back-transformation into E. coli. Nucleic Acids Res. 18: 5319.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5319
    • Ward, A.C.1
  • 54
    • 0025930734 scopus 로고
    • Posttranslational processing of the pro-hormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway
    • Wikox, C.A., and R.S. Fuller. 1991. Posttranslational processing of the pro-hormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathway. J. Cell Biol. 115:297-307.
    • (1991) J. Cell Biol. , vol.115 , pp. 297-307
    • Wikox, C.A.1    Fuller, R.S.2
  • 55
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.