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Src family kinases (Lyn, Fyn, Lck, and Blk) and Syk, a tandem
SH2 domain containing tyrosine kinase, have been demonstrated to be
associated with the antigen receptor in B cells. Both of these
categories of tyrosine kinases are presumed to be critical players in
the process of antigen-mediated signal transduction. Cross-linking of
membrane immunoglobulin on the surface of B cells leads to the
activation of Lyn, Fyn, and Blk, which presumably associate with the
cytoplasmic tails of the membrane immunoglobulin-associated
Ig
/
heterodimer. Receptor ligation also leads to the tyrosine
phosphorylation and catalytic activation of Syk, but the mechanism of
association of this kinase with the antigen receptor remains to be
established. A number of phosphoproteins that can associate with the
SH2 domains of Blk, Lyn, and Fyn have been described in activated B
cells. We demonstrate here that Syk is one of the proteins in the
lysates of activated B cells which bind to the SH2 domains of Src
family kinases. Syk binds directly to the SH2 domain of Blk and
complexes in vivo with Lyn and Blk in activated B cells.
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