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Science 15 May 1992:
Vol. 256. no. 5059, pp. 1031 - 1033
DOI: 10.1126/science.1317058
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Articles

Science, Vol 256, Issue 5059, 1031-1033
Copyright © 1992 by American Association for the Advancement of Science

articles

A site on rod G protein alpha subunit that mediates effector activation

HM Rarick, NO Artemyev, and HE Hamm

Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.

The heterotrimeric guanine nucleotide binding proteins (G proteins) are activated by sensory or hormone receptors. In turn, the G proteins activate effector proteins such as adenylyl cyclase, cyclic guanosine 3',5'-monophosphate phosphodiesterase (cGMP PDE), phospholipase C, and potassium and calcium ion channels by mechanisms that are poorly understood. A site on the alpha subunit of the G protein transducin (alpha t) has been identified that interacts with and activates cGMP phosphodiesterase, the effector enzyme in rod photoreceptors. A 22-amino acid peptide, corresponding to residues 293 to 314 from the COOH-terminal region of alpha t, fully mimicked alpha t and potently activated PDE. This region is adjacent to the receptor activation domain; thus, the alpha subunit of this G protein has a site for interaction with both its effector and receptor that maps near the COOH-terminus.


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