Elimination of Defective α-Factor Pheromone Receptors

REFERENCES

• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Benito, B., E. Riballo, and R. Lagunas. 1991. Turnover of the K1 transport system in Saccharomyces cerevisiae. FEBS Lett. 294:35–37.
   PubMedGoogle Scholar
• Bergeron, J. J. M., M. B. Brenner, D. Y. Thomas, and D. B. Williams. 1994. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19:124–128.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Blumer, K. J., J. E. Reneke, and J. Thorner. 1988. The STE2 gene product is the ligand-binding component of the a-factor receptor of Saccharomyces cerevisiae. J. Biol. Chem. 263:10836–10842.
   PubMedGoogle Scholar
• Burkholder, A. C., and L. H. Hartwell. 1985. The yeast a-factor receptor: structural properties deduced from the sequence of the STE2 gene. Nucleic Acids Res. 13:8463–8475.
   PubMed Web of Science ®Google Scholar
• Cartwright, C. P., Y. Li, Y.-S. Zhu, Y.-S. Kang, and D. J. Tipper. 1994. Use of b-lactamase as a secreted reporter of promoter function in yeast. Yeast 10:497–508.
   PubMedGoogle Scholar
• Cartwright, C. P., and D. J. Tipper. 1991. In vivo topological analysis of Ste2,a yeast plasma membrane protein, by using b-lactamase gene fusions. Mol. Cell. Biol. 11:2620–2628.
   PubMedGoogle Scholar
• Chang, A., and G. R. Fink. 1995. Targeting of the yeast plasma membrane [H1]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J. Cell. Biol. 128:39–49.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Galchevagargova, Z., S. J. Theroux, and R. J. Davis. 1995. The epidermal growth factor receptor is covalently linked to ubiquitin. Oncogene 11:2649–2655.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Hartwell, L. H. 1967. Macromolecule synthesis in temperature-sensitive mutants of yeast. J. Bacteriol. 93:1662–1670.
   PubMed Web of Science ®Google Scholar
• Hartwell, L. H. 1980. Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J. Cell Biol. 85:811–822.
   PubMed Web of Science ®Google Scholar
• Hicke, L., and H. Riezman. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277–287.
   PubMed Web of Science ®Google Scholar
• Hiller, M. M., A. Finger, M. Schweiger, and D. H. Wolf. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273:1725–1728.
   PubMed Web of Science ®Google Scholar
• Hirschman, J., G. DeZutter, W. Simonds, and D. D. Jenness. 1997. The Gbg complex of the yeast pheromone response pathway: subcellular fractionation and protein-protein interaction. J. Biol. Chem. 272:240–248.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Jenness, D. D., A. C. Burkholder, and L. H. Hartwell. 1983. Binding of a-factor pheromone to yeast a cells: chemical and genetic evidence for an a-factor receptor. Cell 35:521–529.
   PubMed Web of Science ®Google Scholar
• Jenness, D. D., A. C. Burkholder, and L. H. Hartwell. 1986. Binding of a-factor pheromone to yeast a cells: dissociation constant and number of binding sites. Mol. Cell. Biol. 6:318–320.
   PubMedGoogle Scholar
• Jenness, D. D., B. S. Goldman, and L. H. Hartwell. 1987. Saccharomyces cerevisiae mutants unresponsive to a-factor pheromone: a-factor binding and extragenic suppression. Mol. Cell. Biol. 7:1311–1319.
   PubMedGoogle Scholar
• Jenness, D. D., and P. Spatrick. 1986. Down regulation of the a-factor pheromone receptor in S. cerevisiae. Cell 46:345–353.
   PubMedGoogle Scholar
• Jones, E. W. 1984. The synthesis and function of proteases in Saccharomyces: genetic approaches. Annu. Rev. Genet. 18:233–270.
   PubMed Web of Science ®Google Scholar
• 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.
   Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Kolling, R., and C. P. Hollenberg. 1994. The ABC-transporter Ste6 accumu-lates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13:3261–3271.
   PubMedGoogle Scholar
• Konopka, J. B., D. D. Jenness, and L. H. Hartwell. 1988. The C-terminus of the S. cerevisiae a-pheromone receptor mediates an adaptive response to pheromone. Cell 54:609–620.
   PubMedGoogle Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Li, Y., P. Spatrick, and D. D. Jenness. Unpublished data.
   Google Scholar
• Manolson, M. F., D. Proteau, R. A. Preston, A. Stenbit, B. T. Roberts, M. A. Hoyt, D. Preuss, J. Mulholland, D. Botstein, and E. W. Jones. 1992. The VPH1 gene encodes a 95-kDa integral membrane polypeptide required for in vivo assembly and activity of the yeast vacuolar H1 ATPase. J. Biol. Chem. 267:14294–14303.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Nakayama, N., A. Miyajima, and K. Arai. 1985. Nucleotide sequences of STE2 and STE3, cell type-specific sterile genes from Saccharomyces cerevi-siae. EMBO J. 4:2643–2648.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Parlati, F., M. Domínguez, 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.
   PubMedGoogle Scholar
• Pringle, J. R., A. E. M. Adams, D. G. Drubin, and B. K. Haarer. 1991. Immunofluorescence methods for yeast. Methods Enzymol. 194:565–602.
   PubMedGoogle Scholar
• Rohrer, J., H. Benedetti, B. Zanolari, and H. Riezman. 1993. Identification of a novel sequence mediating regulated endocytosis of the G-protein coupled a-pheromone receptor in yeast. Mol. Biol. Cell 4:511–521.
   PubMedGoogle Scholar
• Roth, A. F., and N. G. Davis. 1996. Ubiquitination of the yeast a-factor receptor. J. Cell Biol. 134:661–674.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Rothstein, R. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–211.
   PubMed Web of Science ®Google Scholar
• Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281–301.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Schandel, K. A., and D. D. Jenness. 1994. Direct evidence for ligand-induced internalization of the yeast a-factor pheromone receptor. Mol. Cell. Biol. 14:7245–7255.
   PubMed Web of Science ®Google Scholar
• Schultz, J., B. Ferguson, and G. F. Sprague, Jr. 1995. Signal transduction and growth control in yeast. Curr. Opin. Genet. Dev. 5:31–37.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Sommer, T., and S. Jentsch. 1993. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365:176–179.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Strous, G. J., P. van Kerkhof, R. Govers, A. Ciechanover, and A. L. Schwartz. 1996. The ubiquitin conjugation system is required for ligand-induced en-docytosis and degradation of the growth hormone receptor. EMBO J. 15:3806–3812.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Wittenberg, C., and S. I. Reed. 1996. Plugging it in: signaling circuits and the yeast cell cycle. Curr. Opin. Cell Biol. 8:223–230.
   PubMed Web of Science ®Google Scholar