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

doi:10.1016/S0014-5793(99)01424-6

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

Cancer Biology

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	68-72
Number of pages	5
Journal	FEBS Letters
Volume	461
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(99)01424-6
State	Published - Nov 12 1999

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "Bruton's tyrosine kinase (Btk) associates with protein kinase C μ",

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.",

author = "Johannes, {Franz Josef} and Angelika Hausser and Peter Storz and Lars Truckenm{\"u}ller and Gisela Link and Toshiaki Kawakami and Klaus Pfizenmaier",

note = "Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft, Grant no. Jo227/4-3.",

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doi = "10.1016/S0014-5793(99)01424-6",

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T1 - Bruton's tyrosine kinase (Btk) associates with protein kinase C μ

AU - Johannes, Franz Josef

AU - Hausser, Angelika

AU - Storz, Peter

AU - Truckenmüller, Lars

AU - Link, Gisela

AU - Kawakami, Toshiaki

AU - Pfizenmaier, Klaus

N1 - Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft, Grant no. Jo227/4-3.

PY - 1999/11/12

Y1 - 1999/11/12

N2 - 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.

AB - 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.

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ER -

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

Abstract

ASJC Scopus subject areas

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