Agonist-specific conformational changes in the yeast α-factor pheromone receptor

Molecular and Cellular Biology

Volumn 16, Issue 9, 1996, Pages 4818-4823

  Büküşoǧlu, Gül ^a   Jenness, Duane D ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MATING HORMONE ALPHA FACTOR; PHEROMONE; PHEROMONE DERIVATIVE; RECEPTOR;

ARTICLE; CONFORMATIONAL TRANSITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 0029759342     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.9.4818     Document Type: Article

References (52)

1. Ackers, G. K., and J. H. Hazzard. 1993. Transduction of binding energy into hemoglobin cooperativity. Trends Biochem. Sci. 18:385-390.
2. Baldwin, J. M. 1994. Structure and function of receptors coupled to G proteins. Curr. Opin. Cell Biol. 6:180-190.
3. 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.
4. Blinder, D., S. Bouvier, and D. D. Jenness. 1989. Constitutive mutants in the yeast pheromone response: ordered function of the gene products. Cell 56:479-486.
5. 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.
6. 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 α subunit but are required for receptor coupling. Proc. Natl. Acad. Sci. USA 87:4363-4367.
7. 2-adrenoreceptor. Nature (London) 374:272-276.
8. 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.
9. Bukusoglu, G., K. Schandel, and D. D. Jenness. Unpublished data.
10. 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.
11. Chvatchko, Y., I. Howald, and H. Reizman. 1986. Two yeast mutants defective in endocytosis are defective in pheromone response. Cell 46:355-364.
12. 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.
13. Dietzel, C., and J. Kurjan. 1987. The yeast SCG1 gene: a Gα-like protein implicated in the a- and α-factor response pathway. Cell 50:1001-1010.
14. 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.
15. Eriotou-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.
16. Fahmy, K., F. Siebert, and T. P. Sakmar. 1995. Photoactivated state of rhodopsin and how it can form. Biophys. Chem. 56:171-181.
17. Gether, U., S. Lin, and B. K. Kobilka. 1995. Fluorescent labeling of purified adrenergic receptor. Evidence for ligand-specific conformational changes. J. Biol. Chem. 270:28268-28275.
18. Hartwell, L. H. 1967. Macromolecule synthesis in temperature-sensitive mutants of yeast. J. Bacteriol. 93:1662-1670.
19. Hartwell, L. H. 1980. Mutants of Saccharomyces cerevisiae unresponsive to cell division control by polypeptide mating hormone. J. Cell Biol. 85:811-822.
20. 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.
21. 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.
22. Jenness, D. D., and P. Spatrick. 1986. Down regulation of the α-factor pheromone receptor in S. cerevisiae. Cell 46:345-353.
23. König, B. A. Arendt, J. H. McDowell, M. Kahlert, P. A. Hargrave, and K. P. Hofmann. 1989. Three cytoplasmic loops of rhodopsin interact with transducin. Proc. Natl. Acad. Sci. USA 86:6878-6882.
24. Konopka, J. B. 1993. AFR1 acts in conjunction with the α-factor receptor to promote morphogenesis and adaptation. Mol. Cell. Biol. 13:6876-6888.
25. 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.
26. Kühn, H., O. Mommertz, and P. A. Hargrave. 1982. Light-dependent conformational change at rhodopsin's cytoplasmic surface detected by increased susceptibility to proteolysis. Biochim. Biophys. Acta 679:95-100.
27. Luo, X., D. Zhang, and H. Weinstein. 1994. Ligand-induced domain motion in the activation mechanism of a G-protein-coupled receptor. Protein Eng. 7:1441-1448.
28. 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.
29. Marsh, L., A. M. Neiman, and I. Herskowitz. 1991. Signal transduction during pheromone response in yeast. Annu. Rev. Cell Biol. 7:699-728.
30. Monod, J., J. Wyman, and J.-P. Changeux. 1965. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12:88-118.
31. Naider, F., and J. M. Becker. 1986. Structure-activity relationships of the yeast α-factor. Crit. Rev. Biochem. 21:225-248.
32. Pellicone, C., G. Nullans, N. J. Cook, and N. Virmaux. 1985. Light-induced conformational changes in the extradiscal regions of bovine rhodopsin. Biochem. Biophys. Res. Commun. 127:816-821.
33. 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. 1. Biol. Chem. 263:17333-17341.
34. 2-adrenergic receptor. J. Biol. Chem. 268:16483-16487.
35. Reneke, J. E., K. J. Blumer, W. E. Courchesne, and J. Thorner. 1988. The carboxy-terminal segment of the yeast α-factor receptor is a regulatory domain. Cell 55:221-234.
36. 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.
37. 2-adrenergic receptor. J. Biol. Chem. 268: 4625-4636.
38. Schachman, H. K. 1988. Can a simple model account for the allosteric transition of aspartate transcarbamoylase? J. Biol. Chem. 263:18583-18586.
39. 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.
40. Schreiber, R. E., E. R. Prossnitz, R. D. Ye, C. G. Cochrane, and G. M. Bokoch. 1994. Domains of the human neutrophil N-formyl peptide receptor involved in G-protein coupling - mapping with receptor-derived peptides. J. Biol. Chem. 269:326-331.
41. Schultz, J., B. Ferguson, and G. F. Sprague, Jr. 1995. Signal transduction and growth control in yeast. Curr. Opin. Genet. Dev. 5:31-37.
42. Schumacher, M. A., M. M. Dixon, R. Kluger, R. T. Jones, and R. G. Brennan. 1995. Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature (London) 375:84-87.
43. Segall, J. E. 1993. Polarization of yeast cells in spatial gradients of α mating factor. Proc. Natl. Acad. Sci. USA 90:8332-8336.
44. Shenbagamurthi, P., R. Baffi, S. A. Khan, P. Lipke, C. Pousman, J. M. Becker, and F. Naider. 1983. Structure-activity relationships in the dodecapeptide α factor of Saccharomyces cerevisiae. Biochemistry 22:1298-1304.
45. 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.
46. Strader, C. D., T. M. Fong, M. P. Graziano, and M. R. Tota. 1995. The family of G-protein-coupled receptors. FASEB J. 9:745-754.
47. Strader, C. D., T. M. Fong, M. R. Tota, and D. Underwood. 1994. Structure and function of G protein-coupled receptors. Annu. Rev. Biochem. 63:101-132.
48. Taylor, J. M., and R. R. Neubig. 1994. Peptides as probes for G protein signal transduction. Cell. Signalling 6:841-849.
49. 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.
50. Weiss, E. R., D. J. Kelleher, and G. L. Johnson. 1988. Mapping sites of interaction between rhodopsin and transducin using rhodopsin antipeptide antibodies. J. Biol. Chem. 263:6150-6154.
51. 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.
52. Zhang, D., and H. Weinstein. 1993. Signal transduction by a 5-HT2 receptor: a mechanistic hypothesis from molecular dynamics simulations of the three-dimensional model of the receptor complexed to ligands. J. Med. Chem. 36:934-938.