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J Biol Chem, Vol. 275, Issue 18, 13746-13754, May 5, 2000

Gbeta 5gamma 2 Is a Highly Selective Activator of Phospholipid-dependent Enzymes*

Udo MaierDagger §, Aleksei BabichDagger , Nathalie Macrez, Daniela LeopoldtDagger ||, Peter Gierschik**, Daria Illenberger**, and Bernd NürnbergDagger Dagger Dagger

From the Dagger  Institut für Pharmakologie, Freie Universität Berlin, Thielallee 69-73, 14195 Berlin (Dahlem), Germany, the  Laboratoire de Physiologie Cellulaire et Pharmacologie Moléculaire, CNRS UMR 5017, Université de Bordeaux II, 146 rue Léo Saignat, 33076 Bordeaux, France, and the ** Abteilung Pharmakologie und Toxikologie, Universität Ulm, Albert-Einstein-Allee 11, 89081 Ulm, Germany

In this study, Gbeta specificity in the regulation of Gbeta gamma -sensitive phosphoinositide 3-kinases (PI3Ks) and phospholipase Cbeta (PLCbeta ) isozymes was examined. Recombinant mammalian Gbeta 1-3gamma 2 complexes purified from Sf9 membranes stimulated PI3Kgamma lipid kinase activity with similar potency (10-30 nM) and efficacy, whereas transducin Gbeta gamma was less potent. Functionally active Gbeta 5gamma 2 dimers were purified from Sf9 cell membranes following coexpression of Gbeta 5 and Ggamma 2-His. This preparation as well as Gbeta 1gamma 2-His supported pertussis toxin-mediated ADP-ribosylation of Galpha i1. Gbeta 1gamma 2-His stimulated PI3Kgamma lipid and protein kinase activities at nanomolar concentrations, whereas Gbeta 5gamma 2-His had no effect. Accordingly, Gbeta 1gamma 2-His, but not Gbeta 5gamma 2-His, significantly stimulated the lipid kinase activity of PI3Kbeta in the presence or absence of tyrosine-phosphorylated peptides derived from the p85-binding domain of the platelet derived-growth factor receptor. Conversely, both preparations were able to stimulate PLCbeta 2 and PLCbeta 1. However, Gbeta 1gamma 2-His, but not Gbeta 5gamma 2-His, activated PLCbeta 3. Experimental evidence suggests that the mechanism of Gbeta 5-dependent effector selectivity may differ between PI3K and PLCbeta . In conclusion, these data indicate that Gbeta subunits are able to discriminate among effectors independently of Galpha due to selective protein-protein interaction.

* This work was supported in part by the Deutsche Forschungsgemeinschaft, the Fonds der Chemischen Industrie, and CNRS.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.

§ Recipient of the Stiftung Stipendien-Fonds des Verbandes der Chemischen Industrie.

|| Present address: Dept. of Medicine, University of California, Los Angeles, CA 90095-1786.

Dagger Dagger To whom correspondence should be addressed. Tel.: 49-30-8445-1848; Fax: 49-30-8445-1818; E-mail: bnue@zedat.fu-berlin.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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