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FEBS Lett. 2012 Nov 30;586(23):4070-5. doi: 10.1016/j.febslet.2012.09.040. Epub 2012 Oct 16.

CDPKs are dual-specificity protein kinases and tyrosine autophosphorylation attenuates kinase activity.

Author information

1
Department of Plant Biology, University of Illinois, Urbana, IL 61801, USA.

Abstract

Although calcium-dependent protein kinases (CDPKs or CPKs) are classified as serine/threonine protein kinases, autophosphorylation on tyrosine residues was observed for soybean CDPKβ and several Arabidopsis isoforms (AtCPK4 and AtCPK34). We identified Ser-8, Thr-17, Tyr-24 (in the kinase domain), Ser-304, and Ser-358 as autophosphorylation sites of His(6)-GmCDPKβ. Overall autophosphorylation increased kinase activity with synthetic peptides, but autophosphorylation of Tyr-24 appears to attenuate kinase activity based on studies with the Y24F directed mutant. While much remains to be done, it is clear that several CDPKs are dual-specificity kinases, which raises the possibility that phosphotyrosine signaling may play a role in Ca(2+)/CDPK-mediated processes.

PMID:
23079037
DOI:
10.1016/j.febslet.2012.09.040
[Indexed for MEDLINE]
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