CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex
- PMID: 1996090
- PMCID: PMC369396
- DOI: 10.1128/mcb.11.3.1248-1257.1991
CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex
Abstract
CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells to be fully responsive to RAS proteins. CAP also appears to be required for normal cell morphology and responsiveness to nutrient deprivation and excess. We describe here a molecular and phenotypic analysis of the CAP protein. The N-terminal domain is necessary and sufficient for cellular response to activated RAS protein, while the C-terminal domain is necessary and sufficient for normal cellular morphology and responses to nutrient extremes. Thus, CAP is a novel example of a bifunctional component involved in the regulation of diverse signal transduction pathways.
Similar articles
-
Analysis of the function of the 70-kilodalton cyclase-associated protein (CAP) by using mutants of yeast adenylyl cyclase defective in CAP binding.Mol Cell Biol. 1993 Jul;13(7):4087-97. doi: 10.1128/mcb.13.7.4087-4097.1993. Mol Cell Biol. 1993. PMID: 8391632 Free PMC article.
-
Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe.Mol Biol Cell. 1992 Feb;3(2):167-80. doi: 10.1091/mbc.3.2.167. Mol Biol Cell. 1992. PMID: 1550959 Free PMC article.
-
Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein.Cell. 1990 Apr 20;61(2):319-27. doi: 10.1016/0092-8674(90)90812-s. Cell. 1990. PMID: 2184942
-
Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae.Mol Microbiol. 1999 Sep;33(5):904-18. doi: 10.1046/j.1365-2958.1999.01538.x. Mol Microbiol. 1999. PMID: 10476026 Review.
-
Coregulation of starch degradation and dimorphism in the yeast Saccharomyces cerevisiae.Crit Rev Biochem Mol Biol. 1997;32(5):405-35. doi: 10.3109/10409239709082675. Crit Rev Biochem Mol Biol. 1997. PMID: 9383611 Review.
Cited by
-
Actin-induced hyperactivation of the Ras signaling pathway leads to apoptosis in Saccharomyces cerevisiae.Mol Cell Biol. 2006 Sep;26(17):6487-501. doi: 10.1128/MCB.00117-06. Mol Cell Biol. 2006. PMID: 16914733 Free PMC article.
-
Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.J Biol Chem. 2023 Dec;299(12):105367. doi: 10.1016/j.jbc.2023.105367. Epub 2023 Oct 19. J Biol Chem. 2023. PMID: 37863260 Free PMC article.
-
Basidiomycetous ras cDNA functionally replaces its homolog genes in yeast.Curr Genet. 1994 Jan;25(1):30-3. doi: 10.1007/BF00712963. Curr Genet. 1994. PMID: 8082162
-
Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis.Mol Cell Biol. 1999 Jun;19(6):4480-94. doi: 10.1128/MCB.19.6.4480. Mol Cell Biol. 1999. PMID: 10330187 Free PMC article.
-
Mutational analysis of yeast profilin.Mol Cell Biol. 1993 Dec;13(12):7864-73. doi: 10.1128/mcb.13.12.7864-7873.1993. Mol Cell Biol. 1993. PMID: 8247001 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous