Mutation of Unique Region of Bruton's Tyrosine Kinase in Immunodeficient XID Mice

David J. Rawlings(University of California, Los Angeles), Douglas C. Saffran(University of California, Los Angeles), Satoshi Tsukada(Howard Hughes Medical Institute), David A. Largaespada(Cancer Research Center), J. Christopher Grimaldi(Merck & Co., Inc., Rahway, NJ, USA (United States)), Lucie Cohen(Howard Hughes Medical Institute), Randolph N. Mohr(University of California, Los Angeles), J. Fernando Bazán(Merck & Co., Inc., Rahway, NJ, USA (United States)), Maureen Howard(Merck & Co., Inc., Rahway, NJ, USA (United States)), Neal G. Copeland(Houston Methodist), Nancy A. Jenkins(Houston Methodist), Owen N. Witte(Howard Hughes Medical Institute)
Science
July 16, 1993
Cited by 867

Abstract

The cytoplasmic tyrosine kinase, Bruton's tyrosine kinase (Btk, formerly bpk or atk), is crucial for B cell development. Loss of kinase activity results in the human immunodeficiency, X-linked agammaglobulinemia, characterized by a failure to produce B cells. In the murine X-linked immunodeficiency (XID), B cells are present but respond abnormally to activating signals. The Btk gene, btk, was mapped to the xid region of the mouse X chromosome by interspecific backcross analysis. A single conserved residue within the amino terminal unique region of Btk was mutated in XID mice. This change in xid probably interferes with normal B cell signaling mediated by Btk protein interactions.


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