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Originally published In Press as doi:10.1074/jbc.M212145200 on January 13, 2003

J. Biol. Chem., Vol. 278, Issue 12, 10282-10290, March 21, 2003
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Role of the Ca2+/Phosphatidylserine Binding Region of the C2 Domain in the Translocation of Protein Kinase Calpha to the Plasma Membrane*

Stephen R. BolsoverDagger , Juan C. Gomez-Fernandez§, and Senena Corbalan-Garcia§

From the Dagger  Department of Physiology, University College London, Gower St., London WC1E 6BT, United Kingdom and § Departamento de Bioquímica y Biología Molecular (A), Facultad de Veterinaria, Universidad de Murcia, Apartado 4021, E-30100 Murcia, Spain

Signal transduction via protein kinase C (PKC) is closely regulated by its subcellular localization. To map the molecular determinants mediating the C2 domain-dependent translocation of PKCalpha to the plasma membrane, full-length native protein and several point mutants in the Ca2+/phosphatidylserine-binding site were tagged with green fluorescent protein and transiently expressed in rat basophilic leukemia cells (RBL-2H3). Substitution of several aspartate residues by asparagine completely abolished Ca2+-dependent membrane targeting of PKCalpha . Strikingly, these mutations enabled the mutant proteins to translocate in a diacylglycerol-dependent manner, suggesting that neutralization of charges in the Ca2+ binding region enables the C1 domain to bind diacylglycerol. In addition, it was demonstrated that the protein residues involved in direct interactions with acidic phospholipids play differential and pivotal roles in the membrane targeting of the enzyme. These findings provide new information on how the C2 domain-dependent membrane targeting of PKCalpha occurs in the presence of physiological stimuli.

* This work was supported by from Dirección General de Enseñanza Superior e Investigación Científica (Spain) Grant PB98-0389, Dirección General de Investigación (Spain) Grant BM(2002-00119), a grant from Fundación Séneca (Comunidad Autónoma de Murcia), Programa Ramón y Cajal from Ministerio de Ciencia y Tecnologia (Spain) (to S. C.-G.), a short-term fellowship from The Wellcome Trust (to S. C.-G.), and The Wellcome Trust and Medical Research Council (UK) grants (to S. B.).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.

To whom correspondence should be addressed. Tel.: 34-968-364775; Fax: 34-968-364766; E-mail: senena@um.es.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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