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Volumn 20, Issue 14, 2000, Pages 5350-5359

Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; CASEIN KINASE I;

EID: 0033934481     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.14.5350-5359.2000     Document Type: Article
Times cited : (93)

References (52)
  • 2
    • 0027300621 scopus 로고
    • cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein
    • Andres, D. A., M. C. Seabra, M. S. Brown, S. A. Armstrong, T. E. Smeland, F. P. Cremers, and J. L. Goldstein. 1993. cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein. Cell 73:1091-1099.
    • (1993) Cell , vol.73 , pp. 1091-1099
    • Andres, D.A.1    Seabra, M.C.2    Brown, M.S.3    Armstrong, S.A.4    Smeland, T.E.5    Cremers, F.P.6    Goldstein, J.L.7
  • 3
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels, D. J., D. A. Mitchell, X. Dong, and R. J. Deschenes. 1999. Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:6775-6787.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 4
    • 0028953787 scopus 로고
    • Ras membrane targeting is essential for glucose signaling but not for viability in yeast
    • Bhattacharya, S., L. Chen, J. R. Broach, and S. Powers. 1995. Ras membrane targeting is essential for glucose signaling but not for viability in yeast. Proc. Natl. Acad. Sci. USA 92:2984-2988.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2984-2988
    • Bhattacharya, S.1    Chen, L.2    Broach, J.R.3    Powers, S.4
  • 5
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino, J. S., and A. M. Weissman. 1998. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu. Rev. Cell Dev. Biol. 14:19-57.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 6
    • 12044260162 scopus 로고
    • Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype
    • Boone, C., N. G. Davis, and G. F. Sprague, Jr. 1993. Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype. Proc. Natl. Acad. Sci. USA 90:9921-9925.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9921-9925
    • Boone, C.1    Davis, N.G.2    Sprague G.F., Jr.3
  • 7
    • 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 G.F., Jr.3
  • 8
    • 0033960961 scopus 로고    scopus 로고
    • Feedback phosphorylation of the yeast a-factor receptor requires activation of the downstream signaling pathway from G protein through mitogen-activated protein kinase
    • Feng, Y., and N. G. Davis. 2000. Feedback phosphorylation of the yeast a-factor receptor requires activation of the downstream signaling pathway from G protein through mitogen-activated protein kinase. Mol. Cell. Biol. 20:563-574.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 563-574
    • Feng, Y.1    Davis, N.G.2
  • 9
    • 0025731508 scopus 로고
    • Role of acidic residues as substrate determinants for casein kinase I
    • Flotow, H., and P. J. Roach. 1991. Role of acidic residues as substrate determinants for casein kinase I. J. Biol. Chem. 266:3724-3727.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3724-3727
    • Flotow, H.1    Roach, P.J.2
  • 10
    • 0030855771 scopus 로고    scopus 로고
    • The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors
    • Givan, S. A., and G. F. Sprague, Jr. 1997. The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors. Mol. Biol. Cell. 8:1317-1327.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1317-1327
    • Givan, S.A.1    Sprague G.F., Jr.2
  • 11
    • 0029994841 scopus 로고    scopus 로고
    • A new efficient gene disruption cassette for repeated use in budding yeast
    • Guldener, U., S. Heck, T. Fielder, J. Beinhauer, and J. H. Hegemann. 1996. A new efficient gene disruption cassette for repeated use in budding yeast. Nucleic Acids Res. 24:2519-2524.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2519-2524
    • Guldener, U.1    Heck, S.2    Fielder, T.3    Beinhauer, J.4    Hegemann, J.H.5
  • 12
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J. F., H. Paterson, and C. J. Marshall. 1990. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 63:133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 13
    • 0033166078 scopus 로고    scopus 로고
    • Recognition of sorting signals by clathrin adaptors
    • Heilker, R., M. Spiess, and P. Crottet. 1999. Recognition of sorting signals by clathrin adaptors. Bioessays 21:558-567.
    • (1999) Bioessays , vol.21 , pp. 558-567
    • Heilker, R.1    Spiess, M.2    Crottet, P.3
  • 14
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke, L. 1999. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9:107-112.
    • (1999) Trends Cell Biol. , vol.9 , pp. 107-112
    • Hicke, L.1
  • 15
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke, L., and H. Riezman. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 16
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization
    • Hicke, L., B. Zanolari, and H. Riezman. 1998. Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization. J. Cell. Biol. 141:349-58.
    • (1998) J. Cell. Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 17
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 18
    • 0033565639 scopus 로고    scopus 로고
    • Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast
    • Huang, K. M., K. D'Hondt, H. Riezman, and S. K. Lemmon. 1999. Clathrin functions in the absence of heterotetrameric adaptors and AP180-related proteins in yeast. EMBO J. 18:3897-3908.
    • (1999) EMBO J. , vol.18 , pp. 3897-3908
    • Huang, K.M.1    D'Hondt, K.2    Riezman, H.3    Lemmon, S.K.4
  • 19
    • 0028214981 scopus 로고
    • Identification of yeast component a: Reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p
    • Jiang, Y., and S. Ferro-Novick. 1994. Identification of yeast component A: reconstitution of the geranylgeranyltransferase that modifies Ypt1p and Sec4p. Proc. Natl. Acad. Sci. USA 91:4377-4381.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4377-4381
    • Jiang, Y.1    Ferro-Novick, S.2
  • 20
    • 0029655984 scopus 로고    scopus 로고
    • Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae
    • Kao, L. R., J. Peterson, R. Ji, L. Bender, and A. Bender. 1416. Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:168-178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 168-178
    • Kao, L.R.1    Peterson, J.2    Ji, R.3    Bender, L.4    Bender, A.5
  • 22
    • 0024833061 scopus 로고
    • Saccharomyces cerevisiae STE6 gene product: A novel pathway for protein export in eukaryotic cells
    • Kuchler, K., R. E. Sterne, and J. Thorner. 1989. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO J. 8:3973-3984.
    • (1989) EMBO J. , vol.8 , pp. 3973-3984
    • Kuchler, K.1    Sterne, R.E.2    Thorner, J.3
  • 23
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease
    • Marchal, C., R. Haguenauer-Tsapis, and D. Urban-Grimal. 1998. A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease. Mol. Cell. Biol. 18:314-321.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 314-321
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 24
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman, I. 1996. Endocytosis and molecular sorting. Annu. Rev. Cell Dev. Biol. 12:575-625.
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 26
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis, S, and I. Herskowitz. 1988. The a-factor pheromone of Saccharomyces cerevisiae is essential for mating. Mol. Cell. Biol. 8:1309-1318.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 27
    • 0032572759 scopus 로고    scopus 로고
    • The WASp homologue Las17p functions with the WIP homologue End5p/ verprolin and is essential for enducytosis in yeast
    • Naqvi, S. N., R. Zahn, D. A. Mitchell, B. J. Stevenson, and A. L. Munn. 1998. The WASp homologue Las17p functions with the WIP homologue End5p/ verprolin and is essential for enducytosis in yeast. Curr. Biol. 8:959-962.
    • (1998) Curr. Biol. , vol.8 , pp. 959-962
    • Naqvi, S.N.1    Zahn, R.2    Mitchell, D.A.3    Stevenson, B.J.4    Munn, A.L.5
  • 28
    • 0030743354 scopus 로고    scopus 로고
    • Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex
    • Panek, H. R., J. D. Stepp, H. M. Engle, K. M. Marks, P. K. Tan, S. K. Lemmon, and L. C. Robinson. 1997. Suppressors of YCK-encoded yeast casein kinase 1 deficiency define the four subunits of a novel clathrin AP-like complex. EMBO J. 16:4194-4204.
    • (1997) EMBO J. , vol.16 , pp. 4194-4204
    • Panek, H.R.1    Stepp, J.D.2    Engle, H.M.3    Marks, K.M.4    Tan, P.K.5    Lemmon, S.K.6    Robinson, L.C.7
  • 29
    • 0023891818 scopus 로고
    • Protein transport to the vacuole and receptor-mediated endocytosis by clathrin heavy chain-deficient yeast
    • Payne, G. S., D. Baker, E. van Tuinen, and R. Schekman. 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.S.1    Baker, D.2    Van Tuinen, E.3    Schekman, R.4
  • 30
    • 0027455339 scopus 로고
    • end3 and end4: Two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae
    • Raths, S., J. Rohrer, F. Crausaz, and H. Riezman. 1993. end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae. J. Cell Biol. 120:55-65.
    • (1993) J. Cell Biol. , vol.120 , pp. 55-65
    • Raths, S.1    Rohrer, J.2    Crausaz, F.3    Riezman, H.4
  • 31
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and S. W. Rogers. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21:267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 32
    • 0032911043 scopus 로고    scopus 로고
    • The Yck2 yeast casein kinase I isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization
    • Robinson, L. C., C. Bradley, J. D. Bryan, A. Jerome, Y. Kweon, and H. R. Panek. 1999. The Yck2 yeast casein kinase I isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization. Mol. Biol. Cell. 10:1077-1092.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1077-1092
    • Robinson, L.C.1    Bradley, C.2    Bryan, J.D.3    Jerome, A.4    Kweon, Y.5    Panek, H.R.6
  • 33
    • 0027168362 scopus 로고
    • Casein kinase 1-like protein kinases encoded by YCK1 and YCK2 are required for yeast morphogenesis
    • Robinson, L. C., M. M. Menold, S. Garrett, and M. R. Culbertson. 1993. Casein kinase 1-like protein kinases encoded by YCK1 and YCK2 are required for yeast morphogenesis. Mol. Cell. Biol. 13:2870-2881.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2870-2881
    • Robinson, L.C.1    Menold, M.M.2    Garrett, S.3    Culbertson, M.R.4
  • 34
    • 0034677991 scopus 로고    scopus 로고
    • Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor
    • Roth, A. F., and N. G. Davis. 2000. Ubiquitination of the PEST-like endocytosis signal of the yeast a-factor receptor. J. Biol. Chem. 275:8143-8153.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8143-8153
    • Roth, A.F.1    Davis, N.G.2
  • 35
    • 0029781462 scopus 로고    scopus 로고
    • Ubiquitination of the yeast a-factor receptor
    • Roth, A. F., and N. G. Davis. 1996. Ubiquitination of the yeast a-factor receptor. J. Cell Biol. 134:661-674.
    • (1996) J. Cell Biol. , vol.134 , pp. 661-674
    • Roth, A.F.1    Davis, N.G.2
  • 36
    • 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., D. M. Sullivan, and N. G. Davis. 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
  • 37
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-211.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 38
    • 0027362032 scopus 로고
    • Prenylation of Rab5 is dependent on guanine nucleotide binding
    • Sanford, J. C., Y. Pan, and M. Wessling-Resnick. 1993. Prenylation of Rab5 is dependent on guanine nucleotide binding. J. Biol. Chem. 268:23773-23776.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23773-23776
    • Sanford, J.C.1    Pan, Y.2    Wessling-Resnick, M.3
  • 39
    • 0029031685 scopus 로고
    • Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines
    • Sanford, J. C., Y. Pan, and M. Wessling-Resnick. 1995. Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines. Mol. Biol. Cell 6:71-85.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 71-85
    • Sanford, J.C.1    Pan, Y.2    Wessling-Resnick, M.3
  • 40
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor
    • Schandel, K. A., and D. D. Jenness. 1994. Direct evidence for ligand-induced internalization of the yeast alpha-factor pheromone receptor. Mol. Cell. Biol. 14:7245-7255.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7245-7255
    • Schandel, K.A.1    Jenness, D.D.2
  • 41
    • 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
  • 42
    • 0030010536 scopus 로고    scopus 로고
    • Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab
    • Seabra, M. C. 1996. Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab. J. Biol. Chem. 271:14398-14404.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14398-14404
    • Seabra, M.C.1
  • 43
    • 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
  • 45
    • 0027752442 scopus 로고
    • Clathrin facilitates the internalization of seven transmembrane segment receptors for mating pheromones in yeast
    • Tan, P. K., N. G. Davis, G. F. Sprague, and G. S. Payne. 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
  • 46
    • 0030459065 scopus 로고    scopus 로고
    • The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae
    • Tan, P. K., J. P. Howard, and G. S. Payne. 1996. The sequence NPFXD defines a new class of endocytosis signal in Saccharomyces cerevisiae. J. Cell Biol. 135:1789-1800.
    • (1996) J. Cell Biol. , vol.135 , pp. 1789-1800
    • Tan, P.K.1    Howard, J.P.2    Payne, G.S.3
  • 47
    • 0031603760 scopus 로고    scopus 로고
    • A function for monoubiquitination in the internalization of a G protein-coupled receptor
    • Terrell, J., S. Shih, R. Dunn, and L. Hicke. 1998. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell 1:193-202.
    • (1998) Mol. Cell , vol.1 , pp. 193-202
    • Terrell, J.1    Shih, S.2    Dunn, R.3    Hicke, L.4
  • 48
    • 0028108406 scopus 로고
    • A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast
    • Vancura, A., A. Sessler, B. Leichus, and J. Kuret. 1994. A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast. J. Biol. Chem. 269:19271-19278.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19271-19278
    • Vancura, A.1    Sessler, A.2    Leichus, B.3    Kuret, J.4
  • 49
    • 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 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 50
    • 0029818391 scopus 로고    scopus 로고
    • Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase
    • Wang, X., M. F. Hoekstra, A. J. DeMaggio, N. Dhillon, A. Vancura, J. Kuret, G. C. Johnston, and R. A Singer. 1996. Prenylated isoforms of yeast casein kinase I, including the novel Yck3p, suppress the gcs1 blockage of cell proliferation from stationary phase. Mol. Cell. Biol. 16:5375-5385.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5375-5385
    • Wang, X.1    Hoekstra, M.F.2    DeMaggio, A.J.3    Dhillon, N.4    Vancura, A.5    Kuret, J.6    Johnston, G.C.7    Singer, R.A.8
  • 51
    • 0032145902 scopus 로고    scopus 로고
    • Protein traffic in the yeast endocytic and vacuolar protein sorting pathways
    • Wendland, B., S. D. Emr, and H. Riezman. 1998. Protein traffic in the yeast endocytic and vacuolar protein sorting pathways. Curr. Opin. Cell Biol. 10:513-522.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 513-522
    • Wendland, B.1    Emr, S.D.2    Riezman, H.3
  • 52
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L., and P. J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2


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