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G protein-effector coupling: binding of rod phosphodiesterase inhibitory subunit to transducin


G protein-effector coupling: binding of rod phosphodiesterase inhibitory subunit to transducin



Biochemistry 28(8): 3133-3137



ISSN/ISBN: 0006-2960

PMID: 2545248

DOI: 10.1021/bi00434a003

The cyclic GMP phosphodiesterase of retinal rods is composed of three distinct polypeptides: .alpha. (90 kDa), .beta. (86 kDa), and .gamma. (10 kDa). In this multimeric form, the enzyme is inhibited. It activity is stimulated by the interaction with the GTP-bound form of the T.alpha. subunit of transducin and reversed upon the recombination of the inhibitory .gamma. subunit with the catalytic .alpha.beta. subunit. We show here by a novel coimmunoprecipitation technique that the .gamma. subunit, but not the .alpha.beta. subunit, forms a 1:1 complex with T.alpha. The binding of .gamma. to T.alpha. is nucleotide-dependent and is facilitated by GTP.gamma.S or Gpp(NH)p. This study provides convincing evidence that the T.alpha.-GTP subunit of transducin stimulates phosphodiesterase activity by binding to .gamma. and physically carrying it away from .alpha.beta.

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Accession: 017915586

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