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A more recent version of this article appeared on March 15, 2002
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M108965200v1
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Papers In Press, published online ahead of print January 11, 2002
J. Biol. Chem, 10.1074/jbc.M108965200
Submitted on September 17, 2001
Revised on January 10, 2002
Accepted on January 11, 2002

Interaction of Btk and PKC-theta in platelets: Cross-talk between tyrosine and Serine/threonine kinases

David Crosby and Alastair W. Poole

Department of Pharmacology, University of Bristol, Bristol BS8 1TD

Corresponding Author: a.poole{at}bris.ac.uk

The non-receptor tyrosine kinase Btk has been previously shown to physically and functionally associate with members of the 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-HT 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 vWF/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 non-selective inhibition of PKC activity by bisinolylmaleimide I leads to reduction in Btk activity. We propose a reciprocal feedback interaction between Btk and PKCtheta in platelets, where PKCtheta positively modulates activity of Btk, which in turn feeds back negatively upon PKCtheta .


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