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Science 10 February 1989: Vol. 243. no. 4892, pp. 804 - 807 DOI: 10.1126/science.2536957
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Articles
Science, Vol 243, Issue 4892, 804-807
Copyright © 1989 by American Association for the Advancement of Science
Splice variants of the alpha subunit of the G protein Gs activate both adenylyl cyclase and calcium channels
R Mattera,
MP Graziano,
A Yatani,
Z Zhou,
R Graf,
J Codina,
L Birnbaumer,
AG Gilman,
and
AM Brown
Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030.
Signal transducing guanine nucleotide binding (G) proteins are heterotrimers with different alpha 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 Gs, which stimulates adenylyl cyclase, challenged this concept. However, purified Gs may have four distinct alpha-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 alpha subunit may regulate more than one effector function.
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