메뉴 건너뛰기




Volumn 17, Issue 11, 1997, Pages 6236-6245

Elimination of defective α-factor pheromone receptors

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANE PROTEIN; MATING HORMONE ALPHA FACTOR; PHEROMONE; RECEPTOR; UBIQUITIN;

EID: 0030808571     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.11.6236     Document Type: Article
Times cited : (45)

References (69)
  • 1
    • 0000285111 scopus 로고
    • Topography of glycosylation in yeast: Characterization of GDP-mannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles
    • Abeijon, C., P. Orlean, P. W. Robbins, and C. B. Hirschberg. 1989. Topography of glycosylation in yeast: characterization of GDP-mannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles. Proc. Natl. Acad. Sci. USA 86:6935-6939.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6935-6939
    • Abeijon, C.1    Orlean, P.2    Robbins, P.W.3    Hirschberg, C.B.4
  • 2
    • 0023788651 scopus 로고
    • Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein
    • Aris, J. P., and G. Blobel. 1988. Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein. J. Cell Biol. 107:17-31.
    • (1988) J. Cell Biol. , vol.107 , pp. 17-31
    • Aris, J.P.1    Blobel, G.2
  • 3
    • 0028230738 scopus 로고
    • Ultrastructural analysis of the autophagic process in yeast: Detection of autophagosomes and their characterization
    • Baba, M., K. Takeshige, N. Baba, and Y. Ohsumi. 1994. Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization. J. Cell Biol. 124:903-913.
    • (1994) J. Cell Biol. , vol.124 , pp. 903-913
    • Baba, M.1    Takeshige, K.2    Baba, N.3    Ohsumi, Y.4
  • 4
    • 0028556727 scopus 로고
    • Signal propagation and regulation in the mating pheromone response pathway of the yeast Saccharomyces cerevisiae
    • Bardwell, L., J. G. Cook, C. J. Inouye, and J. Thorner. 1994. Signal propagation and regulation in the mating pheromone response pathway of the yeast Saccharomyces cerevisiae. Dev. Biol. 166:363-379.
    • (1994) Dev. Biol. , vol.166 , pp. 363-379
    • Bardwell, L.1    Cook, J.G.2    Inouye, C.J.3    Thorner, J.4
  • 7
    • 0028117116 scopus 로고
    • Metabolic instability and constitutive endocytosis of STE6. the a-factor transporter of Saccharomyces cerevisiae
    • Berkower, C., D. Loayza, and S. Michaelis. 1994. Metabolic instability and constitutive endocytosis of STE6. the a-factor transporter of Saccharomyces cerevisiae. Mol. Biol. Cell 5:1185-1198.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1185-1198
    • Berkower, C.1    Loayza, D.2    Michaelis, S.3
  • 8
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer, T., C. Volkwein, and T. Sommer. 1996. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15:2069-2076.
    • (1996) EMBO J. , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 9
    • 0023680876 scopus 로고
    • The STE2 gene product is the ligand-binding component of the α-factor receptor of Saccharomyces cerevisiae
    • Blumer, K. J., J. E. Reneke, and J. Thorner. 1988. The STE2 gene product is the ligand-binding component of the α-factor receptor of Saccharomyces cerevisiae. J. Biol. Chem. 263:10836-10842.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10836-10842
    • Blumer, K.J.1    Reneke, J.E.2    Thorner, J.3
  • 10
    • 0022422406 scopus 로고
    • The yeast α-factor receptor: Structural properties deduced from the sequence of the STE2 gene
    • Burkholder, A. C., and L. H. Hartwell. 1985. The yeast α-factor receptor: structural properties deduced from the sequence of the STE2 gene. Nucleic Acids Res. 13:8463-8475.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8463-8475
    • Burkholder, A.C.1    Hartwell, L.H.2
  • 11
    • 0028179130 scopus 로고
    • Use of β-lactamase as a secreted reporter of promoter function in yeast
    • Cartwright, C. P., Y. Li, Y.-S. Zhu, Y.-S. Kang, and D. J. Tipper. 1994. Use of β-lactamase as a secreted reporter of promoter function in yeast. Yeast 10:497-508.
    • (1994) Yeast , vol.10 , pp. 497-508
    • Cartwright, C.P.1    Li, Y.2    Zhu, Y.-S.3    Kang, Y.-S.4    Tipper, D.J.5
  • 12
    • 0026315381 scopus 로고
    • In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using β-lactamase gene fusions
    • Cartwright, C. P., and D. J. Tipper. 1991. In vivo topological analysis of Ste2, a yeast plasma membrane protein, by using β-lactamase gene fusions. Mol. Cell. Biol. 11:2620-2628.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2620-2628
    • Cartwright, C.P.1    Tipper, D.J.2
  • 13
    • 0028795584 scopus 로고
    • +]ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • +]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
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to a specific lysine in a targeted short-lived protein
    • Chau, V., J. W. Tobias, A. Bachmair, D. Marriott, D. J. Ecker, D. K. Gonda, and A. Varshavsky. 1989. A multiubiquitin chain is confined to a specific lysine in a targeted short-lived protein. Science 243:1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 15
    • 0029875385 scopus 로고    scopus 로고
    • Selective uptake of cytosolic, peroxisomal, and plasma membrane proteins into the yeast lysosome for degradation
    • Chiang, H. L., R. Schekman, and S. Hamamoto. 1996. Selective uptake of cytosolic, peroxisomal, and plasma membrane proteins into the yeast lysosome for degradation. J. Biol. Chem. 271:9934-9941.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9934-9941
    • Chiang, H.L.1    Schekman, R.2    Hamamoto, S.3
  • 16
    • 0024150158 scopus 로고
    • Response of yeast a cells to a-factor pheromone: Topology of the receptor and identification of a component of the response pathway
    • Clark, K. L., N. G. Davis, D. K. Wiest, J.-J. Hwang-Shum, and G. F. Sprague, Jr. 1988. Response of yeast a cells to a-factor pheromone: topology of the receptor and identification of a component of the response pathway. Cold Spring Harbor Symp. Quant. Biol. 53:611-620.
    • (1988) Cold Spring Harbor Symp. Quant. Biol. , vol.53 , pp. 611-620
    • Clark, K.L.1    Davis, N.G.2    Wiest, D.K.3    Hwang-Shum, J.-J.4    Sprague Jr., G.F.5
  • 17
    • 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
  • 18
    • 0030041980 scopus 로고    scopus 로고
    • The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole
    • Egner, R., and K. Kuchler. 1996. The yeast multidrug transporter Pdr5 of the plasma membrane is ubiquitinated prior to endocytosis and degradation in the vacuole. FEBS Lett. 378:177-181.
    • (1996) FEBS Lett. , vol.378 , pp. 177-181
    • Egner, R.1    Kuchler, K.2
  • 19
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., S. Sadis, B. P. Monia, P. Boucher, D. J. Ecker, S. T. Crooke, and V. Chau. 1994. Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14:5501-5509.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 20
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J. M.. V. Moreau, B. Andre, C. Volland, and R. Haguenauer-Tsapis. 1996. Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271: 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    Andre, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 21
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalently linked to ubiquitin
    • Galchevagargova, Z., S. J. Theroux, and R. J. Davis. 1995. The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene 11:2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galchevagargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 22
    • 0029953575 scopus 로고    scopus 로고
    • Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway
    • Harding, T. M., A. Hefner-Gravink, M. Thumm, and D. J. Klionsky. 1996. Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway. J. Biol. Chem. 271:17621-17624.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17621-17624
    • Harding, T.M.1    Hefner-Gravink, A.2    Thumm, M.3    Klionsky, D.J.4
  • 23
    • 0014086848 scopus 로고
    • Macromolecule synthesis in temperature-sensitive mutants of yeast
    • Hartwell, L. H. 1967. Macromolecule synthesis in temperature-sensitive mutants of yeast. J. Bacteriol. 93:1662-1670.
    • (1967) J. Bacteriol. , vol.93 , pp. 1662-1670
    • Hartwell, L.H.1
  • 24
    • 0018928567 scopus 로고
    • Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone
    • Hartwell, L. H. 1980. Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J. Cell Biol. 85:811-822.
    • (1980) J. Cell Biol. , vol.85 , pp. 811-822
    • Hartwell, L.H.1
  • 25
    • 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
  • 26
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfoldcd luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M. M., A. Finger, M. Schweiger, and D. H. Wolf. 1996. ER degradation of a misfoldcd luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273:1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 27
    • 0030614451 scopus 로고    scopus 로고
    • The Gβγ complex of the yeast pheromone response pathway: Subcellular fractionation and protein-protein interaction
    • Hirschman, J., G. DeZutter, W. Simonds, and D. D. Jenness. 1997. The Gβγ complex of the yeast pheromone response pathway: subcellular fractionation and protein-protein interaction. J. Biol. Chem. 272:240-248.
    • (1997) J. Biol. Chem. , vol.272 , pp. 240-248
    • Hirschman, J.1    DeZutter, G.2    Simonds, W.3    Jenness, D.D.4
  • 28
    • 0029844569 scopus 로고    scopus 로고
    • Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae
    • Hoffman, M., and H. L. Chiang. 1996. Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 143:1555-1566.
    • (1996) Genetics , vol.143 , pp. 1555-1566
    • Hoffman, M.1    Chiang, H.L.2
  • 29
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong, E., A. R. Davidson, and C. A. Kaiser. 1996. A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135:623-633.
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 30
    • 0031045984 scopus 로고    scopus 로고
    • Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway
    • Jeffers, M., G. A. Taylor, K. M. Weidner, S. Omura, and G. F. Vande Woude. 1997. Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell. Biol. 17:799-808.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 799-808
    • Jeffers, M.1    Taylor, G.A.2    Weidner, K.M.3    Omura, S.4    Vande Woude, G.F.5
  • 31
    • 0021070404 scopus 로고
    • Binding of α-factor pheromone to yeast a cells: Chemical and genetic evidence for an α-factor receptor
    • Jenness, D. D., A. C. Burkholder, and L. H. Hartwell. 1983. Binding of α-factor pheromone to yeast a cells: chemical and genetic evidence for an α-factor receptor. Cell 35:521-529.
    • (1983) Cell , vol.35 , pp. 521-529
    • Jenness, D.D.1    Burkholder, A.C.2    Hartwell, L.H.3
  • 32
    • 0022630554 scopus 로고
    • Binding of α-factor pheromone to yeast a cells: Dissociation constant and number of binding sites
    • Jenness, D. D., A. C. Burkholder, and L. H. Hartwell. 1986. Binding of α-factor pheromone to yeast a cells: dissociation constant and number of binding sites. Mol. Cell. Biol. 6:318-320.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 318-320
    • Jenness, D.D.1    Burkholder, A.C.2    Hartwell, L.H.3
  • 33
    • 0023094283 scopus 로고
    • Saccharomyces cerevisiae mutants unresponsive to α-factor pheromone: α-factor binding and extragenic suppression
    • Jenness, D. D., B. S. Goldman, and L. H. Hartwell. 1987. Saccharomyces cerevisiae mutants unresponsive to α-factor pheromone: α-factor binding and extragenic suppression. Mol. Cell. Biol. 7:1311-1319.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1311-1319
    • Jenness, D.D.1    Goldman, B.S.2    Hartwell, L.H.3
  • 34
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone receptor in S. cerevisiae
    • Jenness, D. D., and P. Spatrick. 1986. Down regulation of the α-factor pheromone receptor in S. cerevisiae. Cell 46:345-353.
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 35
    • 0021697064 scopus 로고
    • The synthesis and function of proteases in Saccharomyces: Genetic approaches
    • Jones, E. W. 1984..The synthesis and function of proteases in Saccharomyces: genetic approaches. Annu. Rev. Genet. 18:233-270.
    • (1984) Annu. Rev. Genet. , vol.18 , pp. 233-270
    • Jones, E.W.1
  • 36
    • 0001979549 scopus 로고    scopus 로고
    • Protein secretion, membrane biogenesis, and endocytosis
    • J. R. Pringle, J. R. Broach, and E. W. Jones (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Kaiser, C. A., R. E. Gimeno, and D. A. Shaywitz. 1997. Protein secretion, membrane biogenesis, and endocytosis, p. 91-227. In J. R. Pringle, J. R. Broach, and E. W. Jones (ed.). The molecular and cellular biology of the yeast Saccharomyces, vol. III. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) The Molecular and Cellular Biology of the Yeast Saccharomyces , vol.3 , pp. 91-227
    • Kaiser, C.A.1    Gimeno, R.E.2    Shaywitz, D.A.3
  • 37
    • 0026640551 scopus 로고
    • Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway
    • Klionsky, D. J., R. Cueva, and D. S. Yaver. 1992. Aminopeptidase I of Saccharomyces cerevisiae is localized to the vacuole independent of the secretory pathway. J. Cell Biol. 119:287-299.
    • (1992) J. Cell Biol. , vol.119 , pp. 287-299
    • Klionsky, D.J.1    Cueva, R.2    Yaver, D.S.3
  • 38
    • 0029817714 scopus 로고    scopus 로고
    • N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
    • Knop, M., N. Hauser, and D. H. Wolf. 1996. N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12:1229-1238.
    • (1996) Yeast , vol.12 , pp. 1229-1238
    • Knop, M.1    Hauser, N.2    Wolf, D.H.3
  • 39
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling, R., and C. P. Hollenberg. 1994. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13:3261-3271.
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 40
    • 0023724429 scopus 로고
    • The C-terminus of 'the S. cerevisiae α-pheromone receptor mediates an adaptive response to pheromone
    • Konopka, J. B., D. D. Jenness, and L. H. Hartwell. 1988. The C-terminus of 'the S. cerevisiae α-pheromone receptor mediates an adaptive response to pheromone. Cell 54:609-620.
    • (1988) Cell , vol.54 , pp. 609-620
    • Konopka, J.B.1    Jenness, D.D.2    Hartwell, L.H.3
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bactcriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bactcriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 0028819235 scopus 로고
    • Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole
    • Lai, K., C. P. Bolognese, S. Swift, and P. McGraw. 1995. Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole. J. Biol. Chem. 270:2525-2534.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2525-2534
    • Lai, K.1    Bolognese, C.P.2    Swift, S.3    McGraw, P.4
  • 43
    • 0029775087 scopus 로고    scopus 로고
    • AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • Leonhard, K., J. M. Herrmann, R. A. Stuart, G. Mannhaupt, W. Neupert, and T. Langer. 1996. AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15:4218-4229.
    • (1996) EMBO J. , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5    Langer, T.6
  • 46
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken, A. A., and J. L. Brodsky. 1996. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132:291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 47
    • 0029946016 scopus 로고    scopus 로고
    • Characterization of the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae
    • Medintz, I., H. Jiang, E. K. Han, W. Cui, and C. A. Michels. 1996. Characterization of the glucose-induced inactivation of maltose permease in Saccharomyces cerevisiae. J. Bacteriol. 178:2245-2254.
    • (1996) J. Bacteriol. , vol.178 , pp. 2245-2254
    • Medintz, I.1    Jiang, H.2    Han, E.K.3    Cui, W.4    Michels, C.A.5
  • 48
    • 0001107597 scopus 로고
    • Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae
    • Nakayama, N., A. Miyajima, and K. Arai. 1985. Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevisiae. EMBO J. 4:2643-2648.
    • (1985) EMBO J. , vol.4 , pp. 2643-2648
    • Nakayama, N.1    Miyajima, A.2    Arai, K.3
  • 49
    • 0029994433 scopus 로고    scopus 로고
    • Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis
    • Ooi, C. E., E. Rabinovich, A. Dancis, J. S. Bonifacino, and R. D. Klausner. 1996. Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis. EMBO J. 15:3515-3523.
    • (1996) EMBO J. , vol.15 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2    Dancis, A.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 50
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
    • Parlati, F., M. Dominguez, J. J. M. Bergeron, and D. Y. Thomas. 1995. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270:244-253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 52
    • 0027207946 scopus 로고
    • Identification of a novel sequence mediating regulated endocytosis of the G-protein coupled α-pheromone receptor in yeast
    • Rohrer, J., H. Benedetti, B. Zanolari, and H. Riezman. 1993. Identification of a novel sequence mediating regulated endocytosis of the G-protein coupled α-pheromone receptor in yeast. Mol. Biol. Cell 4:511-521.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 511-521
    • Rohrer, J.1    Benedetti, H.2    Zanolari, B.3    Riezman, H.4
  • 53
    • 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
  • 54
    • 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
  • 55
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein, R. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202-211.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.1
  • 56
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 57
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S. L., K. M. Whitfield, J. P. Vogel, M. D. Rose, and R. W. Schekman. 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69:353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 58
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast α-factor pheromone receptor
    • Schandel, K. A., and D. D. Jenness. 1994. Direct evidence for ligand-induced internalization of the yeast α-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
  • 60
    • 0029913505 scopus 로고    scopus 로고
    • Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
    • Scott, S. V., A. Hefnergravink, K. A. Morano, T. Noda, Y. Ohsumi, and D. J. Klionsky. 1996. Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc. Natl. Acad. Sci. USA 93:12304-12308.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12304-12308
    • Scott, S.V.1    Hefnergravink, A.2    Morano, K.A.3    Noda, T.4    Ohsumi, Y.5    Klionsky, D.J.6
  • 61
    • 0030222298 scopus 로고    scopus 로고
    • Receptor signalling and the regulation of endocytic membrane transport
    • Seaman, M. N., C. G. Burd, and S. D. Emr. 1996. Receptor signalling and the regulation of endocytic membrane transport. Curr. Opin. Cell Biol. 8:549-556.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 549-556
    • Seaman, M.N.1    Burd, C.G.2    Emr, S.D.3
  • 62
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short lived and abnormal proteins
    • Seufert, W., and S. Jentsch. 1990. Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short lived and abnormal proteins. EMBO J. 9:543-550.
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 63
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T., and S. Jentsch. 1993. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365:176-179.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 64
    • 0019719619 scopus 로고
    • Control of yeast cell type by the mating type locus. I. Identification and control of expression of the a-specific gene BAR1
    • Sprague, G. F., Jr., and I. Herskowitz. 1981. Control of yeast cell type by the mating type locus. I. Identification and control of expression of the a-specific gene BAR1. J. Mol. Biol. 153:305-321.
    • (1981) J. Mol. Biol. , vol.153 , pp. 305-321
    • Sprague Jr., G.F.1    Herskowitz, I.2
  • 65
    • 0029765099 scopus 로고    scopus 로고
    • The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor
    • Strous, G. J., P. van Kerkhof, R. Govers, A. Ciechanover, and A. L. Schwartz. 1996. The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15: 3806-3812.
    • (1996) EMBO J. , vol.15 , pp. 3806-3812
    • Strous, G.J.1    Van Kerkhof, P.2    Govers, R.3    Ciechanover, A.4    Schwartz, A.L.5
  • 66
    • 0026668042 scopus 로고
    • Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction
    • Takeshige, K., M. Baba, S. Tsuboi, T. Noda, and Y. Ohsumi. 1992. Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction. J. Cell Biol. 119:301-311.
    • (1992) J. Cell Biol. , vol.119 , pp. 301-311
    • Takeshige, K.1    Baba, M.2    Tsuboi, S.3    Noda, T.4    Ohsumi, Y.5
  • 67
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 68
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E. J. H. J., T. R. Jones, L. Sun, M. Bogyo, H. J. Geuze, and H. L. Ploegh. 1996. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84:769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 69
    • 0029914238 scopus 로고    scopus 로고
    • Plugging it in: Signaling circuits and the yeast cell cycle
    • Wittenberg, C., and S. I. Reed. 1996. Plugging it in: signaling circuits and the yeast cell cycle. Curr. Opin. Cell Biol. 8:223-230.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 223-230
    • Wittenberg, C.1    Reed, S.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.