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Volumn 14, Issue 5, 1994, Pages 3339-3349

The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; HORMONE ANTAGONIST; HORMONE RECEPTOR; HORMONE RECEPTOR STIMULATING AGENT; MATING HORMONE ALPHA FACTOR; PHEROMONE;

EID: 0028273467     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.14.5.3339     Document Type: Article
Times cited : (71)

References (53)
  • 1
    • 0024729959 scopus 로고
    • Regulation of postreceptor signaling in the pheromone response pathway of Saccharomyces cerevisiae
    • Blinder, D., and D. D. Jenness. 1989. Regulation of postreceptor signaling in the pheromone response pathway of Saccharomyces cerevisiae Mol. Cell. Biol. 9:3720-3726.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3720-3726
    • Blinder, D.1    Jenness, D.D.2
  • 2
    • 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
  • 3
    • 0025441553 scopus 로고
    • β and γ subunits of a yeast guanine nudeotide-binding are not essential for membrane association of the α subunit but are required for receptor coupling
    • Blumer, K. J., and J. Thorner. 1990. β and γ subunits of a yeast guanine nudeotide-binding are not essential for membrane association of the α subunit but are required for receptor coupling. Proc. Natl. Acad. Sci. USA 87:4363-4367.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4363-4367
    • Blumer, K.J.1    Thorner, J.2
  • 4
    • 0026080521 scopus 로고
    • Receptor-G protein signalling in yeast
    • Blumer, K. J., and J. Thorner. 1991. Receptor-G protein signalling in yeast. Annu. Rev. Physiol. 53:37-57.
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 37-57
    • Blumer, K.J.1    Thorner, J.2
  • 5
    • 0022422406 scopus 로고
    • The yeast alpha-factor receptor: Structural properties deduced from the sequence of the STE2 gene
    • Burkholder, A. C., and L. H. Harhvell. 1985. The yeast alpha-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    Harhvell, L.H.2
  • 7
    • 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
  • 8
    • 0020040057 scopus 로고
    • Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones
    • Chan, R. K., and C. A. Otte. 1982. Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones. Mol. Cell. Biol. 2:11-20.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 11-20
    • Chan, R.K.1    Otte, C.A.2
  • 9
    • 0020039329 scopus 로고
    • Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and a factor pheromones
    • Chan, R. K., and C. A. Otte. 1982. Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and a factor pheromones. Mol. Cell. Biol. 2:21-29.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 21-29
    • Chan, R.K.1    Otte, C.A.2
  • 10
    • 0025316096 scopus 로고
    • Separation of the structural requirements for agonist-promoted activation and sequestration of the beta-adrenergic receptor
    • Cheung, A. H., R. A. Dixon, W. S. Hill, I. S. Sigal, and C. D. Strader. 1990. Separation of the structural requirements for agonist-promoted activation and sequestration of the beta-adrenergic receptor. Mol. Pharmacol. 37:775-779.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 775-779
    • Cheung, A.H.1    Dixon, R.A.2    Hill, W.S.3    Sigal, I.S.4    Strader, C.D.5
  • 13
    • 0025212680 scopus 로고
    • Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • Cotecchia, S., S. Exum, M. G. Caron, and R. J. Leikowitz. 1990. Regions of the alpha 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA 87:2896-2900.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Leikowitz, R.J.4
  • 15
    • 0023460928 scopus 로고
    • Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: A model for desensitization to pheromone
    • Dietzel, C., and J. Kurjan. 1987. Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone. Mol. Cell. Biol. 7:4169-4177.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4169-4177
    • Dietzel, C.1    Kurjan, J.2
  • 16
    • 85034939049 scopus 로고    scopus 로고
    • Personal communication
    • 14a. Dohlman, H., and J. Thorner. Personal communication.
    • Dohlman, H.1    Thorner, J.2
  • 17
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmembrane segment receptors
    • Dohlman, H. G., J. Thorner, M. G. Caron, and R. J. Lefkowitz. 1991. Model systems for the study of seven-transmembrane segment receptors. Annu. Rev. Biochem. 60:653-688.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 653-688
    • Dohlman, H.G.1    Thorner, J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 18
    • 0026569888 scopus 로고
    • Antagonistic and synergistic peptide analogues of the tridecapeptide mating pheromone of Saccharomyces cerevisiae
    • Eriotu-Bargiota, E., C. B. Xue, F. Naider, and J. M. Becker. 1992. Antagonistic and synergistic peptide analogues of the tridecapeptide mating pheromone of Saccharomyces cerevisiae. Biochemistry 31:551-557.
    • (1992) Biochemistry , vol.31 , pp. 551-557
    • Eriotu-Bargiota, E.1    Xue, C.B.2    Naider, F.3    Becker, J.M.4
  • 19
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin
    • Franke, R. R., T. P. Sakamar, R. M. Graham, and H. G. Khorana. 1992. Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267:14767-14774.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakamar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 20
  • 22
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 23
    • 0022446007 scopus 로고
    • Down-regulation of the α-factor receptor in S. cerevisiae
    • Jenness, D. D., and P. Spatrick. 1986. Down-regulation of the α-factor receptor in S. cerevisiae. Cell 46:345-353.
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 24
    • 0026602063 scopus 로고
    • Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function
    • Khorana, H. G. 1992. Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function. J. Biol. Chem. 267:1-4.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1-4
    • Khorana, H.G.1
  • 25
    • 0025943077 scopus 로고
    • The Schizosaccharomyces pombe mam2 gene encodes a putative pheromone receptor which has a significant homology with the Saccharomyces cerevisiae Ste2 protein
    • Kitamura, K., and C. Shimoda. 1991. The Schizosaccharomyces pombe mam2 gene encodes a putative pheromone receptor which has a significant homology with the Saccharomyces cerevisiae Ste2 protein. EMBO J. 10:3743-3751.
    • (1991) EMBO J. , vol.10 , pp. 3743-3751
    • Kitamura, K.1    Shimoda, C.2
  • 26
    • 0026592357 scopus 로고
    • B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation
    • B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation. J. Biol. Chem. 267:1430-1433.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 27
    • 0023724429 scopus 로고
    • The C-terminus of the Saccharomyces 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 Saccharomyces 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
  • 28
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel, T. A., K. Bebeneck, and J. McClary. 1991. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204:125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebeneck, K.2    McClary, J.3
  • 29
    • 0026637326 scopus 로고
    • Pheromone response in yeast
    • Kurjan, J. 1992. Pheromone response in yeast. Annu. Rev. Biochem. 61:1097-1129.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1097-1129
    • Kurjan, J.1
  • 30
    • 0026734744 scopus 로고
    • Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop
    • Lameh, J., M. Philip, Y. K. Sharma, O. Moro, J. Ramachandran, and W. Saddee. 1992. Hm1 muscarinic cholinergic receptor internalization requires a domain in the third cytoplasmic loop. J. Biol. Chem. 267:13406-13412.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13406-13412
    • Lameh, J.1    Philip, M.2    Sharma, Y.K.3    Moro, O.4    Ramachandran, J.5    Saddee, W.6
  • 31
    • 0025600997 scopus 로고
    • Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes
    • Lechleiter, J., R. Hellmiss, K. Duerson, D. Ennulat, N. David, D. Clapham, and E. Peralta. 1990. Distinct sequence elements control the specificity of G protein activation by muscarinic acetylcholine receptor subtypes. EMBO J. 9:4381-4390.
    • (1990) EMBO J. , vol.9 , pp. 4381-4390
    • Lechleiter, J.1    Hellmiss, R.2    Duerson, K.3    Ennulat, D.4    David, N.5    Clapham, D.6    Peralta, E.7
  • 32
    • 0025045754 scopus 로고
    • Internalization of the Hm1 muscarinic cholinergic receptor involves the third cytoplasmic loop
    • Maeda, S., J. Lameh, W. G. Mallet, M. Philip, J. Ramachandran, and W. Sadee. 1990. Internalization of the Hm1 muscarinic cholinergic receptor involves the third cytoplasmic loop. FEBS Lett. 269:386-388.
    • (1990) FEBS Lett. , vol.269 , pp. 386-388
    • Maeda, S.1    Lameh, J.2    Mallet, W.G.3    Philip, M.4    Ramachandran, J.5    Sadee, W.6
  • 33
    • 0026761601 scopus 로고
    • Substitutions in the hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyveri α-factor and to antagonist
    • Marsh, L. 1992. Substitutions in the hydrophobic core of the α-factor receptor of Saccharomyces cerevisiae permit response to Saccharomyces kluyveri α-factor and to antagonist. Mol. Cell. Biol. 12:3959-3966.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3959-3966
    • Marsh, L.1
  • 34
    • 0024027133 scopus 로고
    • STE2 protein of Saccharomyces kluyveri is a member of the rhodopsin/beta-adrenergic receptor family and is responsible for recognition of the peptide ligand alpha factor
    • Marsh, L., and I. Herskowitz. 1988. STE2 protein of Saccharomyces kluyveri is a member of the rhodopsin/beta-adrenergic receptor family and is responsible for recognition of the peptide ligand alpha factor. Proc. Natl. Acad. Sci. USA 85:3855-3859.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3855-3859
    • Marsh, L.1    Herskowitz, I.2
  • 35
    • 0023395343 scopus 로고
    • Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae
    • McCaffrey, G., F. J. Clay, K. Kelsay, and G. F. Sprague. 1987. Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 7:2680-2690.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2680-2690
    • McCaffrey, G.1    Clay, F.J.2    Kelsay, K.3    Sprague, G.F.4
  • 36
    • 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
  • 37
    • 0025925067 scopus 로고
    • s activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation
    • s activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation. Cell 67:723-730.
    • (1990) Cell , vol.67 , pp. 723-730
    • Okamoto, T.1    Murayama, Y.2    Hayashi, Y.3    Igagaki, M.4    Ogata, E.5    Nishimoto, I.6
  • 39
    • 0024297275 scopus 로고
    • Peptide analogues compete with the binding of α-factor to its receptor in Saccharomyces cerevisiae
    • Raths, S. K., F. Naider, and J. M. Becker. 1988. Peptide analogues compete with the binding of α-factor to its receptor in Saccharomyces cerevisiae. J. Biol. Chem. 263:17333-17341.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17333-17341
    • Raths, S.K.1    Naider, F.2    Becker, J.M.3
  • 40
    • 0024294018 scopus 로고
    • The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain
    • Reneke, J. E., K. J. Blumer, W. E. Courchesne, and J. Thorner. 1988. The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain. Cell 55:221-234.
    • (1988) Cell , vol.55 , pp. 221-234
    • Reneke, J.E.1    Blumer, K.J.2    Courchesne, W.E.3    Thorner, J.4
  • 41
    • 0027413475 scopus 로고
    • Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function
    • Robbins, L. S., J. H. Nadeau, K. R. Johnson, M. A. Kelly, L. Roselli-Rehfuss, E. Baack, K. G. Mountjoy, and R. D. Cone. 1993. Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function. Cell 72:827-834.
    • (1993) Cell , vol.72 , pp. 827-834
    • Robbins, L.S.1    Nadeau, J.H.2    Johnson, K.R.3    Kelly, M.A.4    Roselli-Rehfuss, L.5    Baack, E.6    Mountjoy, K.G.7    Cone, R.D.8
  • 43
    • 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
  • 44
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama, P., S. Cotecchia, T. Costa, and R. J. Lefkowitz. 1993. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 268: 4625-4636.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 45
    • 0024450129 scopus 로고
    • Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: Effects on phosphoinositide metabolism and down-regulation
    • Shapiro, R. A., and N. M. Nathanson. 1989. Deletion analysis of the mouse m1 muscarinic acetylcholine receptor: effects on phosphoinositide metabolism and down-regulation. Biochemistry 28: 8946-8950.
    • (1989) Biochemistry , vol.28 , pp. 8946-8950
    • Shapiro, R.A.1    Nathanson, N.M.2
  • 46
    • 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. Heiter. 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    Heiter, P.2
  • 47
    • 0025971103 scopus 로고
    • Assay of yeast mating reaction
    • Sprague, G. F. 1991. Assay of yeast mating reaction. Methods Enzymol. 194:77-93.
    • (1991) Methods Enzymol. , vol.194 , pp. 77-93
    • Sprague, G.F.1
  • 48
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae
    • E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Sprague, G. F., and J. W. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae, p. 657-744. In E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces, vol. 2. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces , vol.2 , pp. 657-744
    • Sprague, G.F.1    Thorner, J.W.2
  • 49
    • 0025963058 scopus 로고
    • Recovery of plasmids from yeast into Escherichia coli: Shuttle vectors
    • Strathern, J. N., and D. R. Higgins. 1991. Recovery of plasmids from yeast into Escherichia coli: shuttle vectors. Methods Enzymol. 194:319-329.
    • (1991) Methods Enzymol. , vol.194 , pp. 319-329
    • Strathern, J.N.1    Higgins, D.R.2
  • 50
    • 0025280395 scopus 로고
    • Involvement of tyrosine residues located in the carboxyl tail of the human beta 2-adrenergic receptor in agonist-induced down-regulation of the receptor
    • Valiquette, M., H. Bonin, M. Hnatowich, M. G. Caron, R. J. Lefkowitz, and M. Bouvier. 1990. Involvement of tyrosine residues located in the carboxyl tail of the human beta 2-adrenergic receptor in agonist-induced down-regulation of the receptor. Proc. Natl. Acad. Sci. USA 87:5089-5093.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5089-5093
    • Valiquette, M.1    Bonin, H.2    Hnatowich, M.3    Caron, M.G.4    Lefkowitz, R.J.5    Bouvier, M.6
  • 51
    • 0027460543 scopus 로고
    • Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaptation pathway
    • Weiner, J. L., C. Guttierez-Steil, and K. J. Blumer. 1993. Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaptation pathway. J. Biol. Chem. 268: 8070-8077.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8070-8077
    • Weiner, J.L.1    Guttierez-Steil, C.2    Blumer, K.J.3
  • 52
    • 85034941810 scopus 로고    scopus 로고
    • Personal communication
    • Yamamoto, M. Personal communication.
    • Yamamoto, M.1
  • 53
    • 0026493590 scopus 로고
    • Yeast pheromone receptor endocytosis and hyperphosphorylation are independent of G protein-mediated signal transduction
    • Zanolari, B., S. Raths, B. Singer-Kruger, and H. Riezman. 1992. Yeast pheromone receptor endocytosis and hyperphosphorylation are independent of G protein-mediated signal transduction. Cell 71:755-763.
    • (1992) Cell , vol.71 , pp. 755-763
    • Zanolari, B.1    Raths, S.2    Singer-Kruger, B.3    Riezman, H.4


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