Splice variants of the α subunit of the G protein Gs activate both adenylyl cyclase and calcium channels

Rafael Mattera, Michael P. Graziano, Atsuko Yatani, Zhimin Zhou, Rolf Graf, Juan Codina, Lutz Birnbaumer, Alfred G. Gilman, Arthur M. Brown

Research output: Contribution to journalArticlepeer-review

142 Scopus citations


Signal transducing guanine nucleotide binding (G) proteins are heterotrimers with different α subunits that confer specificity for interactions with receptors and effectors. Eight to ten such G proteins couple a large number of receptors for hormones and neurotransmitters to at least eight different effectors. Although one G protein can interact with several receptors, a given G protein was thought to interact with but one effector. The recent finding that voltage-gated calcium channels are stimulated by purified G s, which stimulates adenylyl cyclase, challenged this concept. However, purified Gs may have four distinct α-subunit polypeptides, produced by alternative splicing of messenger RNA. By using recombinant DNA techniques, three of the splice variants were synthesized in Escherichia coli and each variant was shown to stimulate both adenylyl cyclase and calcium channels. Thus, a single G protein α subunit may regulate more than one effector function.

Original languageEnglish (US)
Pages (from-to)804-807
Number of pages4
Issue number4892
StatePublished - 1989

ASJC Scopus subject areas

  • General


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