메뉴 건너뛰기




Volumn 9, Issue 4, 1998, Pages 885-899

Mechanisms governing the activation and trafficking of yeast G protein- coupled receptors

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE RECEPTOR; PHEROMONE; PROLINE;

EID: 0031941108     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.4.885     Document Type: Article
Times cited : (51)

References (68)
  • 1
    • 0023788651 scopus 로고
    • Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein
    • Aris, J.P., and Blobel, G. (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
  • 2
    • 0028143610 scopus 로고
    • The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin
    • Baker, E.K., Colley, N.J., and Zuker, C.S. (1994). The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886-4895.
    • (1994) EMBO J. , vol.13 , pp. 4886-4895
    • Baker, E.K.1    Colley, N.J.2    Zuker, C.S.3
  • 3
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J.M. (1993). The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12, 1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 5
    • 0023680876 scopus 로고
    • The STE2 gene product is the ligand-binding component of the alpha-factor receptor of Saccharomyces cerevisiae
    • Blumer, K.J., Reneke, J.E., and Thorner, J. (1988). The STE2 gene product is the ligand-binding component of the alpha-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
  • 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., Davis, N.G., and Sprague, G.F., 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 Jr., G.F.3
  • 7
    • 0029759342 scopus 로고    scopus 로고
    • Agonist-specific conformational changes in the yeast alpha-factor pheromone receptor
    • Bukusoglu, G., and Jenness, D.D. (1996). Agonist-specific conformational changes in the yeast alpha-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
    • 0028795584 scopus 로고
    • +H]ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • +H]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
  • 9
    • 0025605219 scopus 로고
    • Identification of a gene necessary for cell cycle arrest by a negative growth factor of yeast: FAR1 is an inhibitor of a G1 cyclin, CLN2
    • Chang, F., and Herskowitz, I. (1990). Identification of a gene necessary for cell cycle arrest by a negative growth factor of yeast: FAR1 is an inhibitor of a G1 cyclin, CLN2. Cell 63, 999-1011.
    • (1990) Cell , vol.63 , pp. 999-1011
    • Chang, F.1    Herskowitz, I.2
  • 10
    • 0028286250 scopus 로고
    • Systematic mutagenesis of the yeast mating pheromone receptor third intracellular loop
    • Clark, C.D., Palzkill, T., and Botstein, D. (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
  • 11
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley, N.J., Baker, E.K., Stamnes, M.A., and Zuker, C.S. (1991). The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67, 255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1    Baker, E.K.2    Stamnes, M.A.3    Zuker, C.S.4
  • 12
    • 0028914025 scopus 로고
    • Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration
    • Colley, N.J., Cassill, J.A., Baker, E.K., and Zuker, C.S. (1995). Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration. Proc. Natl. Acad. Sci. USA 92, 3070-3074.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3070-3074
    • Colley, N.J.1    Cassill, J.A.2    Baker, E.K.3    Zuker, C.S.4
  • 13
    • 0028230817 scopus 로고
    • Expanding horizons for receptors coupled to G proteins: Diversity and disease
    • Coughlin, S.R. (1994). Expanding horizons for receptors coupled to G proteins: diversity and disease. Curr. Opin. Cell Biol. 6, 191-197.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 191-197
    • Coughlin, S.R.1
  • 14
    • 0025812324 scopus 로고
    • Model systems for the study of seven-transmembrane-segment receptors
    • Dohlman, H.G., Thorner, J., Caron, M.G. and Lefkowitz, R.J. (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
  • 15
    • 0029767982 scopus 로고    scopus 로고
    • Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: Expression, localization, genetic interaction and physical association with Gpa1 (G protein alpha subunit)
    • Dohlman, H.G., Song, J., Ma, D., Courchesne, W.E., and Thorner, J. (1996). Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization, genetic interaction and physical association with Gpa1 (G protein alpha subunit). Mol. Cell. Biol. 16, 5194-5209.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5194-5209
    • Dohlman, H.G.1    Song, J.2    Ma, D.3    Courchesne, W.E.4    Thorner, J.5
  • 16
    • 0031041306 scopus 로고    scopus 로고
    • RGS proteins and signaling by heterotrimeric G proteins
    • Dohlman, H.G., and Thorner, J. (1997). RGS proteins and signaling by heterotrimeric G proteins. J. Biol. Chem. 272, 3871-3874.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3871-3874
    • Dohlman, H.G.1    Thorner, J.2
  • 17
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Farahbakhsh, Z.T., Hideg, K., and Hubbell, W.L. (1993). Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 262, 1416-1419.
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 18
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D.L., Altenbach, C., Yang, K., Hubbell, W.L. and Khorana, H.G. (1996). Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 19
    • 0029859847 scopus 로고    scopus 로고
    • Cyclophilin-related protein ranbp2 acts as chaperone for red/green opsin
    • Ferreira, P.A., Nakayama, T.A., Pak, W.L., and Travis, G.H. (1996). Cyclophilin-related protein ranbp2 acts as chaperone for red/green opsin. Nature 383, 637-640.
    • (1996) Nature , vol.383 , pp. 637-640
    • Ferreira, P.A.1    Nakayama, T.A.2    Pak, W.L.3    Travis, G.H.4
  • 20
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 21
    • 0026486868 scopus 로고
    • Ocular findings associated with rhodopsin gene codon 267 and codon 190 mutations in dominant retinitis pigmentosa
    • Fishman, G.A., Vandenburgh, K., Stone, E.M., Gilbert, L.D., Alexander, K.R., and Sheffield, V.C. (1992). Ocular findings associated with rhodopsin gene codon 267 and codon 190 mutations in dominant retinitis pigmentosa. Arch. Ophthalmol. 110, 1582-1588.
    • (1992) Arch. Ophthalmol. , vol.110 , pp. 1582-1588
    • Fishman, G.A.1    Vandenburgh, K.2    Stone, E.M.3    Gilbert, L.D.4    Alexander, K.R.5    Sheffield, V.C.6
  • 22
    • 0026886307 scopus 로고
    • Conformational changes of cytosolic loops of bovine rhodopsin during the transition to metarhodopsin-II: An investigation by Fourier transform infrared difference spectroscopy
    • Ganter, U.M., Charitopoulos, T., Virmaux, N., and Siebert, F. (1992). Conformational changes of cytosolic loops of bovine rhodopsin during the transition to metarhodopsin-II: an investigation by Fourier transform infrared difference spectroscopy. J. Pharmacol. Exp. Ther. 56, 57-62.
    • (1992) J. Pharmacol. Exp. Ther. , vol.56 , pp. 57-62
    • Ganter, U.M.1    Charitopoulos, T.2    Virmaux, N.3    Siebert, F.4
  • 23
    • 0027960083 scopus 로고
    • Control of adaptation to mating pheromone by G protein beta subunits of Saccharomyces cerevisiae
    • Grishin, A.V., Weiner, J.L. and Blumer, K.J. (1994). Control of adaptation to mating pheromone by G protein beta subunits of Saccharomyces cerevisiae. Genetics 138, 1081-1092.
    • (1994) Genetics , vol.138 , pp. 1081-1092
    • Grishin, A.V.1    Weiner, J.L.2    Blumer, K.J.3
  • 24
    • 0031047328 scopus 로고    scopus 로고
    • Roles of transmembrane prolines and proline-induced kinks in the lutropin/ choriogonadotropin receptor
    • Hong, S., Ryu, K.-S., Oh, M.-S., Ji, I., and Ji, T.H. (1997). Roles of transmembrane prolines and proline-induced kinks in the lutropin/ choriogonadotropin receptor. J. Biol. Chem. 272, 4166-4171.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4166-4171
    • Hong, S.1    Ryu, K.-S.2    Oh, M.-S.3    Ji, I.4    Ji, T.H.5
  • 25
    • 0026052120 scopus 로고
    • S. cerevisiae alpha pheromone receptors activate a novel signal transduction pathway for mating partner discrimination
    • Jackson, C.L., Konopka, J.B. and Hartwell, L.H. (1991). S. cerevisiae alpha 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
  • 26
    • 0030808571 scopus 로고    scopus 로고
    • Elimination of of defective α-factor pheromone receptors
    • Jenness, D.D., Li, Y., Tipper, C., and Spatrick, P. (1997). Elimination of of defective α-factor pheromone receptors. Mol. Cell. Biol. 17, 6236-6245.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6236-6245
    • Jenness, D.D.1    Li, Y.2    Tipper, C.3    Spatrick, P.4
  • 27
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal, S., and Khorana, H.G. (1994). Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33, 6121-6128.
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 28
    • 0026592357 scopus 로고
    • Constitutive activation of the alpha 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation
    • Kjelsberg, M.A., Cotecchia, S., Ostrowski, J., Caron, M.G., and Lefkowitz, R.J. (1992). Constitutive activation of the alpha 1B-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
  • 30
    • 0029046606 scopus 로고
    • Probing the message-address sites for chemoattractant binding to the C5a receptor - Mutagenesis of hydrophilic and proline residues within the transmembrane segments
    • Kolakowski, L.F., Lu, B., Gerard, C., and Gerard, N.P. (1995). Probing the message-address sites for chemoattractant binding to the C5a receptor - mutagenesis of hydrophilic and proline residues within the transmembrane segments. J. Biol. Chem. 270, 18077-18082.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18077-18082
    • Kolakowski, L.F.1    Lu, B.2    Gerard, C.3    Gerard, N.P.4
  • 31
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling, R., and Hollenberg, C.P. (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
    • Kölling, R.1    Hollenberg, C.P.2
  • 32
    • 0023724429 scopus 로고
    • The C-terminus of the S. cerevisiae alpha-pheromone receptor mediates an adaptive response to pheromone
    • Konopka, J.B., Jenness, D.D., and Hartwell, L.H. (1988). The C-terminus of the S. cerevisiae alpha-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 alpha-factor receptor
    • Konopka, J.B., Margarit, S.M., and Dube, P. (1996). Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-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, S.M.2    Dube, P.3
  • 34
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R.J., Cotecchia, S., Samama, P., and Costa, T. (1993). Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14, 303-307.
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 35
    • 0029756165 scopus 로고    scopus 로고
    • Specific tryptophan uv-absorbance changes are probes of the transition of rhodopsin to its active state
    • Lin, S.W., and Sakmar, T.P. (1996). Specific tryptophan uv-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry 35, 11149-11159.
    • (1996) Biochemistry , vol.35 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 36
    • 0023395343 scopus 로고
    • Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae
    • McCaffrey, G., Clay, F.J., Kelsay, K., and Sprague, G.F., Jr. (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 Jr., G.F.4
  • 38
    • 0023893103 scopus 로고
    • Mechanism of agonist and antagonist binding to alpha 2-adrenergic receptors: Evidence for a precoupled receptor-guanine nucleotide protein complex
    • Neubig, R.R., Gantzos, R.D., and Thomsen, W.J. (1988). Mechanism of agonist and antagonist binding to alpha 2-adrenergic receptors: evidence for a precoupled receptor-guanine nucleotide protein complex. Biochemistry 27, 2374-2784.
    • (1988) Biochemistry , vol.27 , pp. 2374-2784
    • Neubig, R.R.1    Gantzos, R.D.2    Thomsen, W.J.3
  • 39
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functionas as a constituent of the ER quality control apparatus
    • Parlati, F., Dominguez, M., Bergeron, J.J.M., and Thomas, D.Y. (1995). Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functionas 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
  • 40
    • 0027369421 scopus 로고
    • Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas
    • Parma, J., Duprez, L., Van, S.J., Cochaux, P., Gervy, C., Mockel, J., Dumont, J., and Vassart, G. (1993). Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature 365, 649-651.
    • (1993) Nature , vol.365 , pp. 649-651
    • Parma, J.1    Duprez, L.2    Van, S.J.3    Cochaux, P.4    Gervy, C.5    Mockel, J.6    Dumont, J.7    Vassart, G.8
  • 41
    • 0026848828 scopus 로고
    • Minimum energy conformations of proline-containing helices
    • Polinsky, A., Goodman, M., Williams, K.A., and Deber, C.M. (1992). Minimum energy conformations of proline-containing helices. Biopolymers 32, 399-406.
    • (1992) Biopolymers , vol.32 , pp. 399-406
    • Polinsky, A.1    Goodman, M.2    Williams, K.A.3    Deber, C.M.4
  • 43
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J.C., and Pelham, H.R. (1997). Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16, 1832-1841.
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 44
    • 0024294018 scopus 로고
    • The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain
    • Reneke, J.E., Blumer, K.J., Courchesne, W.E., and Thorner, J. (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
  • 45
    • 0027413475 scopus 로고
    • Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function
    • Robbins, L.S., Nadeau, J.H., Johnson, K.R., Kelly, M.A., Roselli, R.L., Baack, E., Mountjoy, K.G., and Cone, R.D. (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, R.L.5    Baack, E.6    Mountjoy, K.G.7    Cone, R.D.8
  • 46
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C.J., Nothwehr, S.F., and Stevens, T.H. (1992). Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J. Cell Biol. 119, 69-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 48
    • 0027207946 scopus 로고
    • Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast
    • Rohrer, J., Benedetti, H., Zanolari, B., and Riezman, H. (1993). Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-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
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M.D., Misra, L.M. and Vogel, J.R. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.R.3
  • 50
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama, P., Cotecchia, S., Costa, T., and Lefkowitz, R.J. (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
  • 51
    • 0027943713 scopus 로고
    • Direct evidence for ligand-induced internalization of the yeast α-factor receptor
    • Schandel, K.A., and Jennesss, D.D. (1994). Direct evidence for ligand-induced internalization of the yeast α-factor receptor. Mol. Cell. Biol. 14, 7245-7255.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7245-7255
    • Schandel, K.A.1    Jennesss, D.D.2
  • 52
    • 0029897495 scopus 로고    scopus 로고
    • Constitutively active mutants of the alpha 1B-adrenergic receptor: Role of highly conserved polar amino acids in receptor activation
    • Scheer, A., Fanelli, F., Costa, T., De, B.P., and Cotecchia, S. (1996). Constitutively active mutants of the alpha 1B-adrenergic receptor: role of highly conserved polar amino acids in receptor activation. EMBO J. 15, 3566-3578.
    • (1996) EMBO J. , vol.15 , pp. 3566-3578
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De, B.P.4    Cotecchia, S.5
  • 53
    • 0027218647 scopus 로고
    • Polarization of yeast cells in spatial gradients of alpha mating factor
    • Segall, J.E. (1993). Polarization of yeast cells in spatial gradients of alpha 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
  • 54
    • 0027372340 scopus 로고
    • A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty
    • Shenker, A., Laue, L., Kosugi, S., Merendino, J.J., Minegishi, T., and Cutler, G.J. (1993). A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature 365, 652-654.
    • (1993) Nature , vol.365 , pp. 652-654
    • Shenker, A.1    Laue, L.2    Kosugi, S.3    Merendino, J.J.4    Minegishi, T.5    Cutler, G.J.6
  • 55
    • 0027939078 scopus 로고
    • Precoupling of alpha-2B adrenergic receptors and G-proteins in transfected PC-12 cell membranes: Influence of pertussis toxin and a lysine-directed cross-linker
    • Shi, A.G., and Deth, R.C. (1994). Precoupling of alpha-2B adrenergic receptors and G-proteins in transfected PC-12 cell membranes: influence of pertussis toxin and a lysine-directed cross-linker. J. Pharmacol. Exp. Ther. 271, 1520-1527.
    • (1994) J. Pharmacol. Exp. Ther. , vol.271 , pp. 1520-1527
    • Shi, A.G.1    Deth, R.C.2
  • 56
    • 0025258519 scopus 로고
    • Interaction between the C5a receptor and Gi in both the membrane-bound and detergent-solubilized states
    • Siciliano, S.J., Rollins, T.E., and Springer, M.S. (1990). Interaction between the C5a receptor and Gi in both the membrane-bound and detergent-solubilized states. J. Biol. Chem. 265, 19568-19574.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19568-19574
    • Siciliano, S.J.1    Rollins, T.E.2    Springer, M.S.3
  • 57
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski, R.S., and Boeke, J.D. (1991). In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194, 302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1    Boeke, J.D.2
  • 58
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae
    • ed. E.W. Jones, J.R. Pringle, and J.R. Broach. Plainview, NY: Cold Spring Harbor Laboratory Press
    • Sprague, G.F. Jr., and Thorner, J.W. (1992) Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae. In: The Molecular and Cellular Biology of the Yeast Saccharomyces, ed. E.W. Jones, J.R. Pringle, and J.R. Broach. Plainview, NY: Cold Spring Harbor Laboratory Press, 657-744.
    • (1992) The Molecular and Cellular Biology of the Yeast Saccharomyces , pp. 657-744
    • Sprague Jr., G.F.1    Thorner, J.W.2
  • 59
    • 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 Blumer, K.J. (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
  • 60
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain
    • Sung, C.H., Davenport, C.M., and Nathans, J. (1993). Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. J. Biol. Chem. 268, 26645-26649.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26645-26649
    • Sung, C.H.1    Davenport, C.M.2    Nathans, J.3
  • 61
    • 0027935666 scopus 로고
    • A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment
    • Sung, C.H., Makino, C., Baylor, D., and Nathans, J. (1994). A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment. J. Neurosci. 14, 5818-5833.
    • (1994) J. Neurosci. , vol.14 , pp. 5818-5833
    • Sung, C.H.1    Makino, C.2    Baylor, D.3    Nathans, J.4
  • 62
    • 0027335690 scopus 로고
    • Precoupling of Gi/G(o)-linked receptors and its allosteric regulation by monovalent cations
    • Tian, W.N., and Deth, R.C. (1993). Precoupling of Gi/G(o)-linked receptors and its allosteric regulation by monovalent cations. Life Sci. 52, 1899-1907.
    • (1993) Life Sci. , vol.52 , pp. 1899-1907
    • Tian, W.N.1    Deth, R.C.2
  • 63
    • 0027460543 scopus 로고
    • Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaptation pathway
    • Weiner, J.L., Guttierez, S.C., and Blumer, K.J. (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, S.C.2    Blumer, K.J.3
  • 64
    • 0027533339 scopus 로고
    • Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor
    • Wess, J., Nanavati, S., Vogel, Z., and Maggio, R. (1993). Functional role of proline and tryptophan residues highly conserved among G protein-coupled receptors studied by mutational analysis of the m3 muscarinic receptor. EMBO J. 12, 331-338.
    • (1993) EMBO J. , vol.12 , pp. 331-338
    • Wess, J.1    Nanavati, S.2    Vogel, Z.3    Maggio, R.4
  • 65
    • 0024966029 scopus 로고
    • The STE4 and STE18 genes of yeast encode potential beta and gamma subunits of the mating factor receptor-coupled G protein
    • Whiteway, M., Hougan, L., Dignard, D., Thomas, D.Y., Bell, L., Saari, G.C., Grant, F.J., O'Hara, P., and MacKay, V.L. (1989). The STE4 and STE18 genes of yeast encode potential beta and gamma subunits of the mating factor receptor-coupled G protein. Cell 56, 467-477.
    • (1989) Cell , vol.56 , pp. 467-477
    • Whiteway, M.1    Hougan, L.2    Dignard, D.3    Thomas, D.Y.4    Bell, L.5    Saari, G.C.6    Grant, F.J.7    O'Hara, P.8    MacKay, V.L.9
  • 66
    • 0027080272 scopus 로고
    • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole
    • Wilcox, C.A., Redding, K., Wright, R., and Fuller, R.S. (1992). Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol. Biol. Cell 3, 1353-1371.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1353-1371
    • Wilcox, C.A.1    Redding, K.2    Wright, R.3    Fuller, R.S.4
  • 67
    • 0025945775 scopus 로고
    • Proline residues in transmembrane helices: Structural or dynamic role?
    • Williams, K.A., and Deber, C.M. (1991). Proline residues in transmembrane helices: structural or dynamic role? Biochemistry 30, 8919-8923.
    • (1991) Biochemistry , vol.30 , pp. 8919-8923
    • Williams, K.A.1    Deber, C.M.2
  • 68
    • 0029680797 scopus 로고    scopus 로고
    • Structure and function in rhodopsin - Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels
    • Yang, K., Farrens, D.L., Altenbach, C., Farahbakhsh, Z.T., Hubbell, W.L. and Khorana, H.G. (1996). Structure and function in rhodopsin - cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels. Biochemistry 35, 14040-14046.
    • (1996) Biochemistry , vol.35 , pp. 14040-14046
    • Yang, K.1    Farrens, D.L.2    Altenbach, C.3    Farahbakhsh, Z.T.4    Hubbell, W.L.5    Khorana, H.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.