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J. Biol. Chem., Vol. 280, Issue 2, 1438-1447, January 14, 2005

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Phospholipase C₂ Binds to and Inhibits Phospholipase C₁^*

Yuanjian Guo, Mario Rebecchi, and Suzanne Scarlata

From the Department of Physiology and Biophysics and the Department of Anesthesiology, State University of New York, Stony Brook, New York 11794-8661

Phospholipase C (PLC) isoforms, which are under the control of G_q and G subunits, generate Ca²⁺ signals induced by a broad array of extracellular agonists, whereas PLC isoforms depend on a rise in cytosolic Ca²⁺ for their activation. Here we find that PLC₂ binds strongly to PLC₁ and inhibits its catalytic activity in vitro and in living cells. In vitro, this PLC complex can be disrupted by increasing concentrations of free G subunits. Such competition has consequences for signaling, because in HEK293 cells PLC₂ suppresses elevated basal [Ca²⁺] and inositol phosphates levels and the sustained agonist-induced elevation of Ca²⁺ levels caused by PLC₁. Also, expression of both PLCs results in a synergistic release of [Ca²⁺] upon stimulation in A10 cells. These results support a model in which PLC₂ suppresses the basal catalytic activity of PLC₁, which is relieved by binding of G subunits to PLC₂ allowing for amplified calcium signals.

Received for publication, July 7, 2004 , and in revised form, October 25, 2004.

^* This work was supported by National Institutes of Health Grants GM53132 (to S. S.) and GM60376 (to M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.

To whom correspondence to should be addressed. Tel.: 631-444-3071; Fax: 631-444-3432; E-mail: Suzanne.Scarlata{at}sunysb.edu.

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