Constitutively active adenylyl cyclase mutant requires neither G proteins nor cytosolic regulators

Carole A. Parent, Peter N. Devreotes

Research output: Contribution to journalArticle

Abstract

Receptor-mediated G protein-linked adenylyl cyclase systems are universal signal transducers. We exploited the essential role of this cascade in Dictyostelium development to screen for random mutations in the catalytic component, ACA. This enzyme is activated by G protein βγ-subunits acting in concert with a novel cytosolic regulator, CRAC. By suppression of the CRAC- null phenotype, we isolated constitutively active versions of the enzyme that require neither exogenous stimuli nor internal regulators. One mutant displayed a 15-fold increase in its V(max). It harbors a single amino acid substitution (L394S) affecting a conserved residue located in the first cytoplasmic loop near the N-terminal hydrophobic domain of ACA. The screening procedure can be adapted for isolation of constitutive mutations in mammalian adenylyl cyclases.

Original languageEnglish (US)
Pages (from-to)18333-18336
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number31
DOIs
StatePublished - Oct 7 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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