메뉴 건너뛰기




Volumn 20, Issue 14, 2000, Pages 5321-5329

The C terminus of the Saccharomyces cerevisiae α-factor receptor contributes to the formation of preactivation complexes with its cognate G protein

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; RECEPTOR;

EID: 0033937183     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.14.5321-5329.2000     Document Type: Article
Times cited : (59)

References (60)
  • 1
    • 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
  • 3
    • 0025441553 scopus 로고
    • β and γ subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the a subunit but are required for receptor coupling
    • Blumer, K. J., and J. Thorner. 1990. β and γ subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the a 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
    • 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
  • 5
    • 0030826705 scopus 로고    scopus 로고
    • A selective inverse agonist for central cannabinoid receptor inhibits mitogen-activated protein kinase activation stimulated by insulin or insulin-like growth factor 1. Evidence for a new model of receptor/ligand interactions
    • Bouaboula, M., S. Perrachon, L. Milligan, X. Canat, M. Rinaldi-Carmona, M. Portier, F. Barth, B. Calandra, F. Pecceu, J. Lupker, J. P. Maffrand, G. Le Fur, and P. Casellas. 1997. A selective inverse agonist for central cannabinoid receptor inhibits mitogen-activated protein kinase activation stimulated by insulin or insulin-like growth factor 1. Evidence for a new model of receptor/ligand interactions. J. Biol. Chem. 272:22330-22339.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22330-22339
    • Bouaboula, M.1    Perrachon, S.2    Milligan, L.3    Canat, X.4    Rinaldi-Carmona, M.5    Portier, M.6    Barth, F.7    Calandra, B.8    Pecceu, F.9    Lupker, J.10    Maffrand, J.P.11    Le Fur, G.12    Casellas, P.13
  • 6
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • Bourne, H. R. 1997. How receptors talk to trimeric G proteins. Curr. Opin. Cell Biol. 9:134-142.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R.1
  • 7
    • 0029759342 scopus 로고    scopus 로고
    • Agonist-specific conformational changes in the yeast α-factor pheromone receptor
    • Bukusoglu, G., and D. D. Jenness. 1996. Agonist-specific conformational changes in the yeast α-factor pheromone receptor. Mol. Cell. Biol. 16:4818-4823.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4818-4823
    • Bukusoglu, G.1    Jenness, D.D.2
  • 8
    • 0029656276 scopus 로고    scopus 로고
    • Regulation of the G protein-coupled α-factor pheromone receptor by phosphorylation
    • Chen, Q., and J. B. Konopka. 1996. Regulation of the G protein-coupled α-factor pheromone receptor by phosphorylation. Mol. Cell. Biol. 16:247-257.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 247-257
    • Chen, Q.1    Konopka, J.B.2
  • 9
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receplor-G protein-effector interactions
    • Chidiac, P. 1998. Rethinking receplor-G protein-effector interactions. Biochem. Pharmacol. 55:549-556.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 10
    • 0028286250 scopus 로고
    • Systematic mutagenesis of the yeast mating pheromone receptor third intracellular loop
    • Clark, C. D., T. Palzkill, and D. Botstein. 1994. Systematic mutagenesis of the yeast mating pheromone receptor third intracellular loop. J. Biol. Chem. 269:8831-8841.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8831-8841
    • Clark, C.D.1    Palzkill, T.2    Botstein, D.3
  • 12
    • 0031705403 scopus 로고    scopus 로고
    • Dominant-negative mutations in the G protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments
    • Dosil, M., L. Giot, C. Davis, and J. B. Konopka. 1998. Dominant-negative mutations in the G protein-coupled α-factor receptor map to the extracellular ends of the transmembrane segments. Mol. Cell. Biol. 18:5981-5991.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5981-5991
    • Dosil, M.1    Giot, L.2    Davis, C.3    Konopka, J.B.4
  • 13
    • 0031724218 scopus 로고    scopus 로고
    • Identification of a polar region in transmembrane domain 6 that regulates the function of the G protein-coupled α-factor receptor
    • Dube, P., and J. B. Konopka. 1998. Identification of a polar region in transmembrane domain 6 that regulates the function of the G protein-coupled α-factor receptor. Mol. Cell. Biol. 18:7205-7215.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7205-7215
    • Dube, P.1    Konopka, J.B.2
  • 14
    • 0031915430 scopus 로고    scopus 로고
    • Edg-2/Vzg-1 couples to the yeast pheromone response pathway selectively in response to lysophosphatidic acid
    • Erickson, J. R., J. J. Wu, J. G. Goddard, G. Tigyi, K. Kawanishi, L. D. Tomei, and M. C. Kiefer. 1998. Edg-2/Vzg-1 couples to the yeast pheromone response pathway selectively in response to lysophosphatidic acid. J. Biol. Chem. 273:1506-1510.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1506-1510
    • Erickson, J.R.1    Wu, J.J.2    Goddard, J.G.3    Tigyi, G.4    Kawanishi, K.5    Tomei, L.D.6    Kiefer, M.C.7
  • 15
    • 0028946950 scopus 로고
    • Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays
    • Ernst, O. P., K. P. Hofmann, and T. P. Sakmar. 1995 Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake. Classification of mutant pigments by fluorescence, nucleotide release, and flash-induced light-scattering assays. J. Biol. Chem. 270:10580-10586.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10580-10586
    • Ernst, O.P.1    Hofmann, K.P.2    Sakmar, T.P.3
  • 17
    • 0025184193 scopus 로고
    • The SPA2 gene of sarcharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating
    • Gehrung, S., and M. Snyder. 1990. The SPA2 gene of Sarcharomyces cerevisiae is important for pheromone-induced morphogenesis and efficient mating. J. Cell. Biol. 111:1451-1464.
    • (1990) J. Cell. Biol. , vol.111 , pp. 1451-1464
    • Gehrung, S.1    Snyder, M.2
  • 18
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II. Mechanism of agonist activation
    • Gether, U., and B. K. Kobilka. 1998. G protein-coupled receptors. II. Mechanism of agonist activation. J. Biol. Chem. 273:17979-17982.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 19
    • 0033618124 scopus 로고    scopus 로고
    • Combining mutations in the incoming and outgoing pheromone signal pathways causes a synergistic mating defect in saccharomyces cerevisiae
    • Giot, L., C. DeMattei, and J. B. Konopka. 1999. Combining mutations in the incoming and outgoing pheromone signal pathways causes a synergistic mating defect in Saccharomyces cerevisiae. Yeast 15:765-780.
    • (1999) Yeast , vol.15 , pp. 765-780
    • Giot, L.1    DeMattei, C.2    Konopka, J.B.3
  • 20
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm, H. E. 1998. The many faces of G protein signaling. J. Biol. Chem. 273:669-672.
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 21
    • 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
  • 22
    • 0030049389 scopus 로고    scopus 로고
    • Two isoforms of the prostaglandin E receptor EP3 subtype different in agonist-independent constitutive activity
    • Hasegawa, H., M. Negishi, and A. Ichikawa. 1996. Two isoforms of the prostaglandin E receptor EP3 subtype different in agonist-independent constitutive activity. J. Biol. Chem. 271:1857-1860.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1857-1860
    • Hasegawa, H.1    Negishi, M.2    Ichikawa, A.3
  • 23
    • 0027982807 scopus 로고
    • Mutational activation of the STE5 gene product bypasses the requirement for g protein β and γ in the yeast pheromone response pathway
    • Hasson, M. S., D. Blinder, J. Thorner, and D. D. Jenness. 1994. Mutational activation of the STE5 gene product bypasses the requirement for G protein β and γ in the yeast pheromone response pathway. Mol. Cell. Biol. 14:1054-1065.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1054-1065
    • Hasson, M.S.1    Blinder, D.2    Thorner, J.3    Jenness, D.D.4
  • 24
    • 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
  • 25
    • 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. 141:349-358.
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 26
    • 0027439219 scopus 로고
    • The pheromone receptors inhibit the pheromone response pathway in Saccharomyces cerevisiae by a process that is independent of their associated gα protein
    • Hirsch, J. P., and F. P. Cross. 1993. The pheromone receptors inhibit the pheromone response pathway in Saccharomyces cerevisiae by a process that is independent of their associated Gα protein. Genetics 135:943-953.
    • (1993) Genetics , vol.135 , pp. 943-953
    • Hirsch, J.P.1    Cross, F.P.2
  • 27
    • 0025598073 scopus 로고
    • Courtship in saccharomyces cerevisiae: Both cell types choose mating partners by responding to the strongest pheromone signal
    • Jackson, C. L., and L. H. Hartwell. 1990. Courtship in Saccharomyces cerevisiae: both cell types choose mating partners by responding to the strongest pheromone signal. Cell 63:1039-1051.
    • (1990) Cell , vol.63 , pp. 1039-1051
    • Jackson, C.L.1    Hartwell, L.H.2
  • 28
    • 0026052120 scopus 로고
    • S. Cerevisiae α-pheromone receptors activate a novel signal transduction pathway for mating partner discrimination
    • Jackson, C. L., J. B. Konopka, and L. H. Hartwell. 1991. S. cerevisiae α-pheromone receptors activate a novel signal transduction pathway for mating partner discrimination. Cell 67:389-402.
    • (1991) Cell , vol.67 , pp. 389-402
    • Jackson, C.L.1    Konopka, J.B.2    Hartwell, L.H.3
  • 29
    • 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
  • 30
    • 0022446007 scopus 로고
    • Down regulation of the α-factor pheromone receptor in saccharomyces cerevisiae
    • Jenness, D. D., and P. Spatrick. 1986. Down regulation of the α-factor pheromone receptor in Saccharomyces cerevisiae. Cell 46:345-353.
    • (1986) Cell , vol.46 , pp. 345-353
    • Jenness, D.D.1    Spatrick, P.2
  • 32
    • 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
  • 33
    • 0029900790 scopus 로고    scopus 로고
    • Mutation of pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled α-factor receptor
    • Konopka, J. B., M. Margarit, and P. Dube. 1996. Mutation of pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled α-factor receptor. Proc. Natl. Acad. Sci. USA 93:6764-6769.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6764-6769
    • Konopka, J.B.1    Margarit, M.2    Dube, P.3
  • 34
    • 0023116389 scopus 로고
    • Fine structure recombinational analysis of cloned genes using yeast transformation
    • Kunes, S., H. Ma, K. Overbye, M. S. Fox, and D. Botstein. 1987. Fine structure recombinational analysis of cloned genes using yeast transformation. Genetics 115:73-81.
    • (1987) Genetics , vol.115 , pp. 73-81
    • Kunes, S.1    H, Ma.2    Overbye, K.3    Fox, M.S.4    Botstein, D.5
  • 35
    • 0030985952 scopus 로고    scopus 로고
    • Changes in the association of G protein subunits with the cloned mouse delta opioid receptor on agonist stimulation
    • Law, S. F., and T. Reisine. 1997. Changes in the association of G protein subunits with the cloned mouse delta opioid receptor on agonist stimulation. J. Pharmacol. Exp. Ther. 281:1476-1486.
    • (1997) J. Pharmacol. Exp. Ther. , vol.281 , pp. 1476-1486
    • Law, S.F.1    Reisine, T.2
  • 36
    • 0027336786 scopus 로고
    • oα selectively associate with the cloned somatostatin receptor subtype SSTR2
    • oα selectively associate with the cloned somatostatin receptor subtype SSTR2. J. Biol. Chem. 268:10721-10727.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10721-10727
    • Law, S.F.1    Yasuda, K.2    Bell, G.I.3    Reisine, T.4
  • 37
    • 0032788711 scopus 로고    scopus 로고
    • Dominant negative mutations in the α-factor receptor, a G protein-coupled receptor encoded by the STE2 gene of the yeast Saccharomyces cerevisiae
    • Leavitt, L. M., C. R. Macaluso, K. S. Kim, N. P. Martin, and M. E. Dumont. 1999. Dominant negative mutations in the α-factor receptor, a G protein-coupled receptor encoded by the STE2 gene of the yeast Saccharomyces cerevisiae. Mol. Gen. Genet. 261:917-932.
    • (1999) Mol. Gen. Genet. , vol.261 , pp. 917-932
    • Leavitt, L.M.1    Macaluso, C.R.2    Kim, K.S.3    Martin, N.P.4    Dumont, M.E.5
  • 38
    • 0031058930 scopus 로고    scopus 로고
    • Pheromone signalling and polarized morphogenesis in yeast
    • Leberer, E., D. Y. Thomas, and M. Whiteway. 1997. Pheromone signalling and polarized morphogenesis in yeast. Curr. Opin. Genet. Dev. 7:59-66.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 59-66
    • Leberer, E.1    Thomas, D.Y.2    Whiteway, M.3
  • 39
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig, R. R. 1994. Membrane organization in G-protein mechanisms. FASEB J. 8:939-946.
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 40
    • 0032076379 scopus 로고    scopus 로고
    • Specificity of receptor-G protein coupling: Protein structure and cellular determinants
    • Neubig, R. R. 1998. Specificity of receptor-G protein coupling: protein structure and cellular determinants. Semin. Neurosci. 9:189-197.
    • (1998) Semin. Neurosci. , vol.9 , pp. 189-197
    • Neubig, R.R.1
  • 41
    • 0029569117 scopus 로고
    • 1α on rhodopsin and guanine nucleotide binding
    • 1α on rhodopsin and guanine nucleotide binding. J. Biol. Chem. 270:31052-31058.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31052-31058
    • Osawa, S.1    Weiss, E.R.2
  • 42
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton, M. C., and K. J. Blumer. 2000. G-protein-coupled receptors function as oligomers in vivo. Curr. Biol. 10:341-344.
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 43
    • 0031543433 scopus 로고    scopus 로고
    • G protein-coupled receptors in Saccharomyces cerevisiae: High-throughput screening assays for drug discovery
    • Pausch, M. H. 1997. G protein-coupled receptors in Saccharomyces cerevisiae: high-throughput screening assays for drug discovery. Trends Biotechnol. 15:487-494.
    • (1997) Trends Biotechnol. , vol.15 , pp. 487-494
    • Pausch, M.H.1
  • 44
    • 0029862555 scopus 로고    scopus 로고
    • 2A-adenosine receptor functionally coupled to the yeast pheromone response pathway
    • 2A-adenosine receptor functionally coupled to the yeast pheromone response pathway. Mol. Pharmacol. 50:829-837.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 829-837
    • Price, L.A.1    Strnad, J.2    Pausch, M.3    Hadcock, J.R.4
  • 45
    • 0024294018 scopus 로고
    • The carboxyl terminal domain of the α-factor receptor is a regulatory domain
    • Reneke, J. E., K. J. Blumer, W. E. Courchesne, and J. Thorner. 1988. The carboxyl terminal domain of the α-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
  • 46
    • 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
  • 49
    • 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
  • 50
    • 0027218647 scopus 로고
    • Polarization of yeast cells in spatial gradients of α-mating factor
    • Segall, J. E. 1993. Polarization of yeast cells in spatial gradients of α-mating factor. Proc. Natl. Acad. Sci. USA 90:8332-8336.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8332-8336
    • Segall, J.E.1
  • 51
    • 0030568847 scopus 로고    scopus 로고
    • Role of SST2 in modulating G protein-coupled receptor signaling
    • Shah, A., and L. Marsh. 1996. Role of SST2 in modulating G protein-coupled receptor signaling. Biochem. Biophys. Res. Commun. 226:242-246.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 242-246
    • Shah, A.1    Marsh, L.2
  • 52
    • 0031581813 scopus 로고    scopus 로고
    • Mechanistic model of G-protein signal transduction. Determinants of efficacy and effect of precoupled receptors
    • Shea, L., and J. J. Linderman. 1997. Mechanistic model of G-protein signal transduction. Determinants of efficacy and effect of precoupled receptors. Biochem. Pharmacol. 53:519-530.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 519-530
    • Shea, L.1    Linderman, J.J.2
  • 53
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 54
    • 0028273467 scopus 로고
    • The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization
    • Stefan, C. J., and K. J. Blumer. 1994. The third cytoplasmic loop of a yeast G-protein-coupled receptor controls pathway activation, ligand discrimination, and receptor internalization. Mol. Cell. Biol. 14:3339-3349.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3339-3349
    • Stefan, C.J.1    Blumer, K.J.2
  • 55
    • 0031941108 scopus 로고    scopus 로고
    • Mechanisms governing the activation and trafficking of yeast G protein-coupled receptors
    • Stefan, C. J., M. C. Overton, and K. J. Blumer. 1998. Mechanisms governing the activation and trafficking of yeast G protein-coupled receptors. Mol. Biol. Cell 9:885-899.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 885-899
    • Stefan, C.J.1    Overton, M.C.2    Blumer, K.J.3
  • 56
    • 0342979873 scopus 로고    scopus 로고
    • The CB1 cannabinoid receptor can sequester G-proteins, making them unavailable to couple to other receptors
    • Vasquez, C., and D. L. Lewis. 1999. The CB1 cannabinoid receptor can sequester G-proteins, making them unavailable to couple to other receptors. J. Neurosci. 19:9271-9280.
    • (1999) J. Neurosci. , vol.19 , pp. 9271-9280
    • Vasquez, C.1    Lewis, D.L.2
  • 58
    • 0027460543 scopus 로고
    • Disruption of receptor-G protein coupling in yeast promotes the function of as SST2-dependent adaptation pathway
    • Weiner, J. L., S. Guttierez-Steil, and K. J. Blunter. 1993. Disruption of receptor-G protein coupling in yeast promotes the function of as 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, S.2    Blunter, K.J.3
  • 59
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of g-protein recognition
    • Wess, J. 1997. G-protein-coupled receptors: molecular mechanisms involved in receptor activation and selectivity of G-protein recognition. FASEB J. 11:346-354.
    • (1997) FASEB J. , vol.11 , pp. 346-354
    • Wess, J.1
  • 60
    • 0032055105 scopus 로고    scopus 로고
    • α subunit and functions in a Ras-independent pathway
    • α subunit and functions in a Ras-independent pathway. EMBO J. 17:1996-2007.
    • (1998) EMBO J. , vol.17 , pp. 1996-2007
    • Xue, Y.1    Batlle, M.2    Hirsch, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.