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Originally published In Press as doi:10.1074/jbc.M205583200 on July 9, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34885-34895, September 20, 2002
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Regulation of Angiotensin II-induced G Protein Signaling by Phosducin-like Protein*

Joseph N. McLaughlin, Craig D. Thulin, Steven M. Bray, Mickey M. Martin, Terry S. Elton, and Barry M. WillardsonDagger

From the Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602

Phosducin-like protein (PhLP) is a broadly expressed member of the phosducin (Pd) family of G protein beta gamma subunit (Gbeta gamma )-binding proteins. Though PhLP has been shown to bind Gbeta gamma in vitro, little is known about its physiological function. In the present study, the effect of PhLP on angiotensin II (Ang II) signaling was measured in Chinese hamster ovary cells expressing the type 1 Ang II receptor and various amounts of PhLP. Up to 3.6-fold overexpression of PhLP had no effect on Ang II-stimulated inositol trisphosphate (IP3) formation, whereas further increases caused an abrupt decrease in IP3 production with half-maximal inhibition occurring at 6-fold PhLP overexpression. This threshold level for inhibition corresponds to the cellular concentration of cytosolic chaperonin complex, a recently described binding partner that preferentially binds PhLP over Gbeta gamma . Results of pertussis toxin sensitivity, GTPgamma S binding, and immunoprecipitation experiments suggest that PhLP inhibits phospholipase Cbeta activation by dual mechanisms: (i) steric blockage of Gbeta gamma activation of PLCbeta and (ii) interference with Gbeta gamma -dependent cycling of Gqalpha by the receptor. These results suggest that G protein signaling may be regulated through controlling the cellular concentration of free PhLP by inducing its expression or by regulating its binding to the chaperonin.

* This work was supported by National Institutes of Health Grants EY12287 (to B. M. W.) and HL48848 (to T. S. E.) and National Science Foundation Grant MCB-0131361 (to B. M. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 801-422-2785; Fax: 801-422-0153; E-mail: barry_willardson@byu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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