CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex

Gerst, J. E., Ferguson, K., Vojtek, A., Wigler, M. H., Field, J. (March 1991) CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Molecular & Cellular Biology, 11 (3). pp. 1248-57. ISSN 0270-7306

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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.

Item Type: Paper
Additional Information:
Uncontrolled Keywords: Adenylate Cyclase genetics Base Sequence Blotting Western Cloning Molecular DNA Mutational Analysis DNA-Binding Proteins Fungal Proteins genetics metabolism Genes Structural Fungal Macromolecular Substances Molecular Sequence Data Oligonucleotides chemistry Protein Kinases Saccharomyces cerevisiae growth & development physiology Saccharomyces cerevisiae Proteins Signal Transduction Structure-Activity Relationship Transcription Factors genetics ras Proteins
Subjects: organism description > yeast > Saccharomyces
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression
CSHL Authors:
Communities: CSHL labs > Wigler lab
Depositing User: CSHL Librarian
Date: March 1991
Date Deposited: 13 Apr 2012 20:20
Last Modified: 08 Nov 2016 21:12
PMCID: PMC369396
Related URLs:
URI: https://repository.cshl.edu/id/eprint/26184

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