Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins

Gang Yu, John Swiston, Dallan Young

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

We previously reported the identification of human CAP, a protein that is related to the Saccharomyces cerevisiae and Schizosaccharomyces pombe adenylyl cyclase-associated CAP proteins. The two yeast CAP proteins have similar functions: the N-terminal domains are required for the normal function of adenylyl cyclase, while loss of the C-terminal domains result in morphological and nutritional defects that are unrelated to the cAMP pathways. We have amplified and cloned cDNAs from a human glioblastoma library that encode a second CAP-related protein, CAP2. The human CAP and CAP2 proteins are 64% identical. Expression of either human CAP or CAP2 in S. cerevisiae cap- strains suppresses phenotypes associated with deletion of the C-terminal domain of CAP, but does not restore hyper-activation of adenylyl cyclase by RAS2(va119). Similarly, expression of either human CAP or CAP2 in S. pombe cap- strains suppresses the morphological and temperature-sensitive phenotypes associated with deletion of the C-terminal domain of CAP in this yeast. In addition, expression of human CAP, but not CAP2, suppresses the propensity to sporulate due to deletion of the N-terminal domain of CAP in S. pombe. This latter observation suggests that human CAP restores normal adenylyl cyclase activity in S. pombe cap- cells. Thus, functional properties of both N-terminal and C-terminal domains are conserved between the human and S. pombe CAP proteins.

Original languageEnglish (US)
Pages (from-to)1671-1678
Number of pages8
JournalJournal of cell science
Volume107
Issue number6
StatePublished - Jun 1 1994

Keywords

  • Actin
  • Adenylyl cyclase
  • CAP
  • RAS

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins'. Together they form a unique fingerprint.

  • Cite this