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Science 22 July 1988:
Vol. 241. no. 4864, pp. 448 - 451
DOI: 10.1126/science.2899356
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Articles

Science, Vol 241, Issue 4864, 448-451
Copyright © 1988 by American Association for the Advancement of Science

articles

Carboxyl terminal domain of Gs alpha specifies coupling of receptors to stimulation of adenylyl cyclase

SB Masters, KA Sullivan, RT Miller, B Beiderman, NG Lopez, J Ramachandran, and HR Bourne

Department of Pharmacology, University of California, San Francisco 94143.

The alpha subunits of Gs and Gi link different sets of hormone receptors to stimulation and inhibition, respectively, of adenylyl cyclase. A chimeric alpha i/alpha s cDNA was constructed that encodes a polypeptide composed of the amino terminal 60% of an alpha i chain and the carboxyl terminal 40% of alpha s. The cDNA was introduced via a retroviral vector into S49 cyc- cells, which lack endogenous alpha s. Although less than half of the hybrid alpha chain is derived from alpha s, its ability to mediate beta-adrenoceptor stimulation of adenylyl cyclase matched that of the normal alpha s polypeptide expressed from the same retroviral vector in cyc- cells. This result indicates that carboxyl terminal amino acid sequences of alpha s contain the structural features that are required for specificity of interactions with the effector enzyme, adenylyl cyclase, as well as with the hormone receptor.


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