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The FASEB Journal, Vol 2, 2841-2848, Copyright © 1988 by The Federation of American Societies for Experimental Biology
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ER Weiss, DJ Kelleher, CW Woon, S Soparkar, S Osawa, LE Heasley and GL Johnson
Department of Biochemistry, University of Massachusetts Medical School, Worcester 01655.
G proteins are a highly conserved family of membrane-associated proteins composed of alpha, beta, and gamma subunits. The alpha subunit, which is unique for each G protein, binds GDP or GTP. Receptors such as those for beta- and alpha-adrenergic catecholamines, muscarinic agonists, and the retinal photoreceptor rhodopsin, catalyze the exchange of GDP for GTP binding to the alpha subunit of a specific G protein. G alpha.GTP regulates appropriate effector enzymes such as adenylyl cyclase or the cyclic GMP phosphodiesterase. The beta gamma- subunit complex of G proteins is required for efficient receptor- catalyzed alpha subunit guanine nucleotide exchange and also functions as an attenuator of alpha subunit activation of effector enzymes. Recent elucidation of both receptor and G protein primary sequence has allowed structural predictions and new experimental approaches to study the mechanism of receptor-catalyzed G protein regulation of specific effector systems and the control of cell function including metabolism, secretion, and growth.
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