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

Mol Cell Biol. 1991 Mar;11(3):1248-57. doi: 10.1128/mcb.11.3.1248-1257.1991.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / genetics*
  • Base Sequence
  • Blotting, Western
  • Cloning, Molecular
  • DNA Mutational Analysis
  • DNA-Binding Proteins*
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Genes, Fungal*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Oligonucleotides / chemistry
  • Protein Kinases*
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins*
  • Signal Transduction
  • Structure-Activity Relationship
  • Transcription Factors / genetics
  • ras Proteins*

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • Macromolecular Substances
  • Oligonucleotides
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Protein Kinases
  • ras Proteins
  • Adenylyl Cyclases