Open AccessBruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells.
Author(s) -
Yoichi Aoki,
Kurt J. Isselbacher,
Shiv Pillai
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.22.10606
Subject(s) - bruton's tyrosine kinase , tyrosine kinase , ror1 , receptor tyrosine kinase , microbiology and biotechnology , tropomyosin receptor kinase c , b cell receptor , biology , tyrosine phosphorylation , x linked agammaglobulinemia , cancer research , b cell , phosphorylation , signal transduction , receptor , biochemistry , platelet derived growth factor receptor , antibody , immunology , growth factor
The gene encoding Bruton tyrosine kinase (Btk) is known to be mutated in human X chromosome-linked agammaglobulinemia and in the Xid mouse. This kinase was examined in B lymphocytes before and after antigen receptor ligation and also in pre-B cells. Btk was found to be catalytically activated and tyrosine phosphorylated in response to anti-IgM stimulation in B cells. This kinase is also constitutively phosphorylated on tyrosine residues in pre-B cells. These findings point to a functional role for Btk in pre-antigen and antigen receptor signaling during B-cell development and provide a biochemical explanation for the X-linked genetic syndromes already linked to this kinase.