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Volumn 13, Issue 12, 2002, Pages 4296-4307

Vps10p cycles between the TGN and the late endosome via the plasma membrane in clathrin mutants

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; CLATHRIN; GREEN FLUORESCENT PROTEIN; PROTEIN; PROTEIN CYP; PROTEIN TGN; PROTEIN VPS 10P; PROTEINASE; UNCLASSIFIED DRUG; CELL SURFACE RECEPTOR; DNA; PEP1 PROTEIN, S CEREVISIAE; PHOTOPROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; VESICULAR TRANSPORT PROTEIN;

EID: 0036911346     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.02-07-0105     Document Type: Article
Times cited : (22)

References (50)
  • 2
    • 0030012162 scopus 로고    scopus 로고
    • Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast
    • Becherer, K.A., Rieder, S.E., Emr, S.D., and Jones, E.W. (1996). Novel syntaxin homologue, Pep12p, required for the sorting of lumenal hydrolases to the lysosome-like vacuole in yeast. Mol. Biol. Cell 7, 579-594.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 579-594
    • Becherer, K.A.1    Rieder, S.E.2    Emr, S.D.3    Jones, E.W.4
  • 3
    • 0034735540 scopus 로고    scopus 로고
    • A selective transport route from Golgi to late endosomes that requires file yeast GGA proteins
    • Black, M.W., and Pelham, H.R. (2000). A selective transport route from Golgi to late endosomes that requires file yeast GGA proteins. J. Cell Biol. 151, 587-600.
    • (2000) J. Cell Biol. , vol.151 , pp. 587-600
    • Black, M.W.1    Pelham, H.R.2
  • 4
    • 0031749473 scopus 로고    scopus 로고
    • Traffic into the prevacuolar/endosomal compartment of Saccharomyces cerevisiae: A VPS45-dependent intracellular route and a VPS45-independent, endocytic route
    • Bryant, N.J., Piper, R.C., Gerrard, S.R., and Stevens, T.H. (1998). Traffic into the prevacuolar/endosomal compartment of Saccharomyces cerevisiae: A VPS45-dependent intracellular route and a VPS45-independent, endocytic route. Eur J. Cell Biol. 76, 43-52.
    • (1998) Eur J. Cell Biol. , vol.76 , pp. 43-52
    • Bryant, N.J.1    Piper, R.C.2    Gerrard, S.R.3    Stevens, T.H.4
  • 5
    • 0030952211 scopus 로고    scopus 로고
    • A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast
    • Burd, C.G., Peterson, M., Cowles, C.R., and Emr, S.D. (1997) A novel Sec18p/NSF-dependent complex required for Golgi-to-endosome transport in yeast. Mol. Biol. Cell 8, 1089-1104.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1089-1104
    • Burd, C.G.1    Peterson, M.2    Cowles, C.R.3    Emr, S.D.4
  • 6
    • 0031595549 scopus 로고    scopus 로고
    • An arf1 Delta synthetic lethal screen identifies a new clathrin heavy chain conditional allele that perturbs vacuolar protein transport in Saccharomyces cerevisiae
    • Chen, C.Y., and Graham, T.R. (1998). An arf1 Delta synthetic lethal screen identifies a new clathrin heavy chain conditional allele that perturbs vacuolar protein transport in Saccharomyces cerevisiae. Genetics 150, 577-589.
    • (1998) Genetics , vol.150 , pp. 577-589
    • Chen, C.Y.1    Graham, T.R.2
  • 7
    • 12644297393 scopus 로고    scopus 로고
    • The light chain subunit is required for clathrin function in Saccharomyces cerevisiae
    • Chu, D.S., Pishvaee, B., and Payne, G.S. (1996). The light chain subunit is required for clathrin function in Saccharomyces cerevisiae. J. Biol. Chem. 271, 33123-33130.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33123-33130
    • Chu, D.S.1    Pishvaee, B.2    Payne, G.S.3
  • 8
    • 0029844403 scopus 로고    scopus 로고
    • Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p
    • Chuang, J.S., and Schekman, R.W. (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.S.1    Schekman, R.W.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 Stevens, T.H. (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
    • 0027175829 scopus 로고
    • Cis- and trans-acting functions required for endocytosis of the yeast pheromone receptors
    • Davis, N.G., Horecka, J.L., and Sprague, G.F., 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 G.F., Jr.3
  • 11
    • 0035155279 scopus 로고    scopus 로고
    • Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles
    • Deloche, O., Yeung, B.G., Payne, G.S., and Schekman, R. (2001). Vps10p transport from the trans-Golgi network to the endosome is mediated by clathrin-coated vesicles. Mol. Biol. Cell 12, 475-485.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 475-485
    • Deloche, O.1    Yeung, B.G.2    Payne, G.S.3    Schekman, R.4
  • 12
    • 0025315397 scopus 로고
    • Antibodies to clathrin inhibit endocytosis but not recycling to the trans Golgi network in vitro
    • Draper, R.K., Goda, Y., Brodsky, F.M., and Pfeffer, S.R. (1990). Antibodies to clathrin inhibit endocytosis but not recycling to the trans Golgi network in vitro. Science 248, 1539-1541.
    • (1990) Science , vol.248 , pp. 1539-1541
    • Draper, R.K.1    Goda, Y.2    Brodsky, F.M.3    Pfeffer, S.R.4
  • 13
    • 0027507707 scopus 로고
    • Structural and functional characterization of Sec66p, a new submit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum
    • Feldheim, D., Yoshimura, K., Admon, A., and Schekman, R. (1993). Structural and functional characterization of Sec66p, a new submit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum. Mol. Biol. Cell 4, 931-939.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 931-939
    • Feldheim, D.1    Yoshimura, K.2    Admon, A.3    Schekman, R.4
  • 14
    • 0026061021 scopus 로고
    • Identification of a novel, N-ethylmaleimide-sensitive cytosolic factor required for vesicular transport from endosomes to the trans-Golgi network in vitro
    • Goda, Y., and Pfeffer, S.R. (1991). Identification of a novel, N-ethylmaleimide-sensitive cytosolic factor required for vesicular transport from endosomes to the trans-Golgi network in vitro. J. Cell Biol. 112, 823-831.
    • (1991) J. Cell Biol. , vol.112 , pp. 823-831
    • Goda, Y.1    Pfeffer, S.R.2
  • 15
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C., and Fink, G.R. (1991). Guide to yeast genetics and molecular biology. Methods Enzymol. 194, 3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Guthrie, C.1    Fink, G.R.2
  • 16
    • 0028787438 scopus 로고
    • Parallel secretory pathways to the cell surface in yeast
    • Harsay, E., and Bretscher, A. (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
  • 17
    • 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 Schekman, R. (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
  • 18
    • 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. (1998a). Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 77, 113-126.
    • (1998) EMBO J. , vol.77 , pp. 113-126
    • Holthuis, J.C.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.4
  • 19
    • 0031795632 scopus 로고    scopus 로고
    • The syntaxin Tlglp mediates trafficking of chitin synthase III to polarized growth sites in yeast
    • Holthuis, J.C., Nichols, B.J., and Pelham, H.R. (1998b). The syntaxin Tlglp mediates trafficking of chitin synthase III to polarized growth sites in yeast. Mol. Biol. Cell 9, 3383-3397.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3383-3397
    • Holthuis, J.C.1    Nichols, B.J.2    Pelham, H.R.3
  • 20
    • 0035032574 scopus 로고    scopus 로고
    • Demonstration in yeast of the function of BP-80, a putative plant vacuolar sorting receptor
    • Humair, D., Hernández Felipe, D., Neuhaus, J.-M., and Paris, N. (2001). Demonstration in yeast of the function of BP-80, a putative plant vacuolar sorting receptor. Plant Cell 13, 781-792.
    • (2001) Plant Cell , vol.13 , pp. 781-792
    • Humair, D.1    Hernández Felipe, D.2    Neuhaus, J.-M.3    Paris, N.4
  • 21
    • 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
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
    • Marcusson, E.G., Horazdovsky, B.F., Cereghino, J.L., Gharakhanian, E., and Emr, S.D. (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
  • 24
    • 0033995518 scopus 로고    scopus 로고
    • Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor
    • Nicoziani, P., Vilhardt, F., Llorente, A., Hilout, L., Courtoy, P.J., Sandvig, K., and van Deurs, B. (2000). Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor. Mol. Biol. Cell 11, 481-495.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 481-495
    • Nicoziani, P.1    Vilhardt, F.2    Llorente, A.3    Hilout, L.4    Courtoy, P.J.5    Sandvig, K.6    Van Deurs, B.7
  • 25
    • 0032910357 scopus 로고    scopus 로고
    • Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment
    • Nothwehr, S.F., Bruinsma, P., and Strawn, L.A. (1999). Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment. Mol. Biol. Cell 10, 875-890.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 875-890
    • Nothwehr, S.F.1    Bruinsma, P.2    Strawn, L.A.3
  • 26
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vpsl mutant yeast cells via the plasma membrane
    • Nothwehr, S.F., Conibear, E., and Stevens, T.H. (1995). Golgi and vacuolar membrane proteins reach the vacuole in vpsl 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
  • 27
    • 0034675999 scopus 로고    scopus 로고
    • Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p
    • Nothwehr, S.F., Ha, S.A., and Bruinsma, P. (2000). Sorting of yeast membrane proteins into an endosome-to-Golgi pathway involves direct interaction of their cytosolic domains with Vps35p. J. Cell Biol. 151, 297-310.
    • (2000) J. Cell Biol. , vol.151 , pp. 297-310
    • Nothwehr, S.F.1    Ha, S.A.2    Bruinsma, P.3
  • 28
    • 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., Roberts, C.J., and Stevens, T.H. (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
  • 29
    • 0023891818 scopus 로고
    • Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast
    • Payne, G., Baker, D., Van Tuinen, E., and Schekman, R. (1988). Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast. J. Cell Biol. 106, 1453-1461.
    • (1988) J. Cell Biol. , vol.106 , pp. 1453-1461
    • Payne, G.1    Baker, D.2    Van Tuinen, E.3    Schekman, R.4
  • 30
    • 0024454653 scopus 로고
    • Clathrin: A role in the intracellular retention of a Golgi membrane protein
    • Payne, G.S., and Schekman, R. (1989). Clathrin: A role in the intracellular retention of a Golgi membrane protein. Science 245, 1358-1365.
    • (1989) Science , vol.245 , pp. 1358-1365
    • Payne, G.S.1    Schekman, R.2
  • 31
    • 0030852699 scopus 로고    scopus 로고
    • The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway
    • Piper, R., Bryant, N., and Stevens, T. (1997). The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. J. Cell Biol. 138, 531-546.
    • (1997) J. Cell Biol. , vol.138 , pp. 531-546
    • Piper, R.1    Bryant, N.2    Stevens, T.3
  • 33
    • 0028904692 scopus 로고
    • Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP beta subunit, plays a role in clathrin-dependent Golgi functions
    • Rad, M.R., Phan, H.L., Kirchrath, L., Tan, P.K., Kirchhausen, T., Hollenberg, C.P., and Payne, G.S. (1995). Saccharomyces cerevisiae Apl2p, a homologue of the mammalian clathrin AP beta subunit, plays a role in clathrin-dependent Golgi functions. J. Cell Sci. 108, 1605-1615.
    • (1995) J. Cell Sci. , vol.108 , pp. 1605-1615
    • Rad, M.R.1    Phan, H.L.2    Kirchrath, L.3    Tan, P.K.4    Kirchhausen, T.5    Hollenberg, C.P.6    Payne, G.S.7
  • 34
    • 0025752784 scopus 로고
    • Immurolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding, K., Holcomb, C., and Fuller, R.S. (1991). Immurolocalization 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
  • 35
    • 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., Seeger, M., Payne, G.S., and Fuller, R.S. (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.1    Seeger, M.2    Payne, G.S.3    Fuller, R.S.4
  • 36
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C.J., Nothwehr, S.F., and Stevens, T.H. (1992). Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment. J. Cell Biol. 119, 69-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 37
    • 0032563560 scopus 로고    scopus 로고
    • A large PEST-like sequence directs the ubiquitination, endocytosis, and vacuolar degradation of the yeast a-factor receptor
    • Roth, A.F., Sullivan, D.M., and Davis, N.G. (1998). A large PEST-like sequence directs the ubiquitination, endocytosis, and vacuolar degradation of the yeast a-factor receptor. J. Cell Biol. 142, 949-961.
    • (1998) J. Cell Biol. , vol.142 , pp. 949-961
    • Roth, A.F.1    Sullivan, D.M.2    Davis, N.G.3
  • 38
    • 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., Raymond, C.K., Gilbert, T., O'Hara, P.J., and Stevens, T.H. (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
  • 39
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R., and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 40
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid, S.L. (1997). Clathrin-coated vesicle formation and protein sorting: An integrated process. Annu. Rev. Biochem. 66, 511-548.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 41
    • 0030897485 scopus 로고    scopus 로고
    • Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products
    • Seaman, M.N., Marcusson, E.G., Cereghino, J.L., and Emr, S.D. (1997). Endosome to Golgi retrieval of the vacuolar protein sorting receptor, Vps10p, requires the function of the VPS29, VPS30, and VPS35 gene products. J. Cell Biol. 137, 79-92.
    • (1997) J. Cell Biol. , vol.137 , pp. 79-92
    • Seaman, M.N.1    Marcusson, E.G.2    Cereghino, J.L.3    Emr, S.D.4
  • 42
    • 0031823307 scopus 로고    scopus 로고
    • A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast
    • Seaman, M.N., McCaffery, J.M., and Emr, S.D. (1998). A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. J., Cell Biol. 142, 665-681.
    • (1998) J. Cell Biol. , vol.142 , pp. 665-681
    • Seaman, M.N.1    McCaffery, J.M.2    Emr, S.D.3
  • 43
    • 0026652588 scopus 로고
    • A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast
    • Seeger, M., and Payne, G.S. (1992). A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast. EMBO J. 11, 2811-2818.
    • (1992) EMBO J. , vol.11 , pp. 2811-2818
    • Seeger, M.1    Payne, G.S.2
  • 44
    • 0025132351 scopus 로고
    • Yeast clathrin has a distinctive light chain that is important for cell growth
    • Silveira, L.A., Wong, D.H., Masiarz, F.R., and Schekman, R. (1990). Yeast clathrin has a distinctive light chain that is important for cell growth. J. Cell Biol. 111, 1437-1449.
    • (1990) J. Cell Biol. , vol.111 , pp. 1437-1449
    • Silveira, L.A.1    Wong, D.H.2    Masiarz, F.R.3    Schekman, R.4
  • 45
    • 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
  • 46
    • 0020181690 scopus 로고
    • Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole
    • Stevens, T., Esmon, B., and Schekman, R. (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
  • 47
    • 0027752442 scopus 로고
    • Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast
    • Tan, P.K., Davis, N.G., Sprague, G.F., and Payne, G.S. (1993). Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast. J. Cell Biol. 123, 1707-1716.
    • (1993) J. Cell Biol. , vol.123 , pp. 1707-1716
    • Tan, P.K.1    Davis, N.G.2    Sprague, G.F.3    Payne, G.S.4
  • 48
    • 0026471712 scopus 로고
    • The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae, is a GTPase with two functionally separable domains
    • Vater, C.A., Raymond, C.K., Ekena, K., Howald-Stevenson, I., and Stevens, T.H. (1992). The VPS1 protein, a homolog of dynamin required for vacuolar protein sorting in Saccharomyces cerevisiae, is a GTPase with two functionally separable domains. J. Cell Biol. 119, 773-786.
    • (1992) J. Cell Biol. , vol.119 , pp. 773-786
    • Vater, C.A.1    Raymond, C.K.2    Ekena, K.3    Howald-Stevenson, I.4    Stevens, T.H.5
  • 49
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida, T.A., and Emr, S.D. (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
  • 50
    • 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., Redding, K., Wright, R., and Fuller, R.S. (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


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