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Research Article

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

J E Gerst, K Ferguson, A Vojtek, M Wigler, J Field
J E Gerst
Cold Spring Harbor Laboratory, New York 11724.
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K Ferguson
Cold Spring Harbor Laboratory, New York 11724.
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A Vojtek
Cold Spring Harbor Laboratory, New York 11724.
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M Wigler
Cold Spring Harbor Laboratory, New York 11724.
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J Field
Cold Spring Harbor Laboratory, New York 11724.
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DOI: 10.1128/MCB.11.3.1248
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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.

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CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex.
J E Gerst, K Ferguson, A Vojtek, M Wigler, J Field
Molecular and Cellular Biology Mar 1991, 11 (3) 1248-1257; DOI: 10.1128/MCB.11.3.1248

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CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex.
J E Gerst, K Ferguson, A Vojtek, M Wigler, J Field
Molecular and Cellular Biology Mar 1991, 11 (3) 1248-1257; DOI: 10.1128/MCB.11.3.1248
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