Bruton's tyrosine kinase (Btk) associates with protein kinase C μ

Franz Josef Johannes, Angelika Hausser, Peter Storz, Lars Truckenmüller, Gisela Link, Toshiaki Kawakami, Klaus Pfizenmaier

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Bruton's tyrosine kinase (Btk) is considered an essential signal transducer in B-cells. Mutational defects are associated with a severe immunodeficiency syndrome, X-chromosome linked agammaglobulinemia (XLA). Here we show by coimmunoprecipitation that a member of the protein kinase C (PKC) family, PKCμ, is constitutively associated with Btk. Neither antigen receptor (Ig) crosslinking nor stimulation of B-cells with phorbol ester or H2O2 affected Btk/PKCμ interaction. GST precipitation analysis revealed association of the Btk pleckstrin/Tec homology domain with PKCμ. Transient overexpression of PKCμ deletion mutants as well as expression of selected PKCμ domains in 293T cells revealed that both the kinase domain and the regulatory C1 region are independently capable of binding to the Btk PH-TH domain. These data show the existence of a PKCμ/Btk complex in vivo and identify two PKCμ domains that participate in Btk interaction.

Original languageEnglish (US)
Pages (from-to)68-72
Number of pages5
JournalFEBS Letters
Volume461
Issue number1-2
DOIs
StatePublished - Nov 12 1999

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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