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Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors.

TitlePhosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors.
Publication TypeJournal Article
Year of Publication1997
AuthorsWahl MI, Fluckiger AC, Kato RM, Park H, Witte ON, Rawlings DJ
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue21
Pagination11526-33
Date Published1997 Oct 14
ISSN0027-8424
Keywords3T3 Cells, Amino Acid Sequence, Animals, Antibodies, Antibody Specificity, B-Lymphocytes, Cell Line, Enzyme Activation, Humans, Mast Cells, Mice, Models, Biological, Molecular Sequence Data, Phosphopeptides, Phosphorylation, Protein-Tyrosine Kinases, Rabbits, Receptors, Antigen, B-Cell, Receptors, IgE, Receptors, Interleukin, Receptors, Interleukin-5, Recombinant Proteins, src Homology Domains, src-Family Kinases, Transfection, Tyrosine, Vaccinia virus
Abstract

Mutation of Bruton's tyrosine kinase (Btk) impairs B cell maturation and function and results in a clinical phenotype of X-linked agammaglobulinemia. Activation of Btk correlates with an increase in the phosphorylation of two regulatory Btk tyrosine residues. Y551 (site 1) within the Src homology type 1 (SH1) domain is transphosphorylated by the Src family tyrosine kinases. Y223 (site 2) is an autophosphorylation site within the Btk SH3 domain. Polyclonal, phosphopeptide-specific antibodies were developed to evaluate the phosphorylation of Btk sites 1 and 2. Crosslinking of the B cell antigen receptor (BCR) or the mast cell Fcepsilon receptor, or interleukin 5 receptor stimulation each induced rapid phosphorylation at Btk sites 1 and 2 in a tightly coupled manner. Btk molecules were singly and doubly tyrosine-phosphorylated. Phosphorylated Btk comprised only a small fraction (

Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID9326643


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