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Originally published In Press as doi:10.1074/jbc.M108965200 on January 11, 2002

J. Biol. Chem., Vol. 277, Issue 12, 9958-9965, March 22, 2002
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Interaction of Bruton's Tyrosine Kinase and Protein Kinase Ctheta in Platelets
CROSS-TALK BETWEEN TYROSINE AND SERINE/THREONINE KINASES*

David Crosby and Alastair W. PooleDagger

From the Department of Pharmacology, School of Medical Sciences, University Walk, Bristol BS8 1TD, United Kingdom

The nonreceptor Bruton's tyrosine kinase (Btk) has been previously shown to associate physically and functionally with members of the protein kinase C (PKC) family of serine/threonine kinases in a variety of cell types. Here we show evidence for a novel interaction between Btk and PKCtheta in platelets activated through the adhesion receptors GP Ib-V-IX and GP VI. Alboaggregin A, a snake venom component capable of activating both receptors in combination, leads to tyrosine phosphorylation of Btk downstream of Src family kinases. Inhibition of Btk by the selective antagonist LFM-A13 causes a reduction in calcium entry, although secretion of 5-hydroxytryptamine is potentiated. Btk is also phosphorylated on threonine residues in a PKC-dependent manner and associates with PKCtheta upon platelet activation by either alboaggregin A or activation of GP Ib-V-IX alone by von Willebrand factor/ristocetin. PKCtheta in turn becomes tyrosine-phosphorylated in a manner dependent upon Src family and Btk kinase activity. Inhibition of Btk activity by LFM-A13 leads to enhancement of PKCtheta activity, whereas nonselective inhibition of PKC activity by bisindolylmaleimide I leads to reduction in Btk activity. We propose a reciprocal feedback interaction between Btk and PKCtheta in platelets, in which PKCtheta positively modulates activity of Btk, which in turn feeds back negatively upon PKCtheta .

* This work was supported by the Medical Research Council (U. K.) and the British Heart Foundation.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.: 44-117-928-7635; Fax: 44-117-925-0168; E-mail: a.poole@bris.ac.uk.

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