Complexity and diversity of mammalian adenylyl cyclases

Roger K. Sunahara, Carmen W. Dessauer, Alfred G. Gilman

Research output: Contribution to journalReview articlepeer-review

740 Scopus citations


Molecular cloning has permitted identification of several novel isoforms of mammalian adenylyl cyclase; these proteins now comprise a family of at least 10. All of the membrane-bound enzymes are activated by the α subunit of G(α), a receptor-regulated, heterotrimeric guanine nucleotide-binding protein, and by the diterpene forskolin. Certain cyclases are also activated by Ca2+-calmodulin, while some are inhibited by the α subunits of the three G(i) proteins. The discovery of new isoforms has also revealed unanticipated mechanisms of regulation, including activation or inhibition by the G-protein βγ subunit complex, inhibition by G(0α), inhibition by Ca2+, and phosphorylation by protein kinases C and A. The effects of activators are often highly synergistic or conditional, suggesting function of these enzymes as coincidence detectors. The plethora of receptors, G proteins, and adenylyl cyclases permits assembly of very complex signaling systems with a wide variety of integrative characteristics.

Original languageEnglish (US)
Pages (from-to)461-480
Number of pages20
JournalAnnual review of pharmacology and toxicology
StatePublished - 1996


  • G proteins
  • adenylyl cyclase
  • calmodulin
  • forskolin
  • phosphorylation

ASJC Scopus subject areas

  • Toxicology
  • Pharmacology


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