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- W2143409212 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, PKCmu, is constitutively associated with Btk. Neither antigen receptor (Ig) crosslinking nor stimulation of B-cells with phorbol ester or H(2)O(2) affected Btk/PKCmu interaction. GST precipitation analysis revealed association of the Btk pleckstrin/Tec homology domain with PKCmu. Transient overexpression of PKCmu deletion mutants as well as expression of selected PKCmu 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 PKCmu/Btk complex in vivo and identify two PKCmu domains that participate in Btk interaction." @default.
- W2143409212 created "2016-06-24" @default.
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- W2143409212 date "1999-11-08" @default.
- W2143409212 modified "2023-10-13" @default.
- W2143409212 title "Bruton's tyrosine kinase (Btk) associates with protein kinase C μ" @default.
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- W2143409212 doi "https://doi.org/10.1016/s0014-5793(99)01424-6" @default.
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