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

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

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.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • Calcium / metabolism*
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism*
  • Immunoblotting
  • Mass Spectrometry
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism*
  • Serine / metabolism
  • Tandem Mass Spectrometry
  • Threonine / metabolism
  • Tyrosine / metabolism*

Substances

  • Arabidopsis Proteins
  • Calcium-Binding Proteins
  • Recombinant Proteins
  • Threonine
  • Tyrosine
  • Serine
  • Protein Serine-Threonine Kinases
  • Calcium