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Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor.


ABSTRACT: Upon B-cell activation, the signaling subunits Ig-? and Ig-? of the B-cell antigen receptor become phosphorylated not only on tyrosines but also on serine residues. Using a specific antibody, we show that serine 197 (S197) in the cytoplasmic tail of Ig-? is phosphorylated upon B-cell antigen receptor activation, and that this modification inhibits the signal output of the B-cell antigen receptor. Surprisingly, we found that the well-known protein tyrosine kinase Syk (spleen tyrosine kinase) phosphorylates S197 on Ig-?, thus not only activating but also inhibiting signaling from the B-cell antigen receptor. This finding identifies Syk as a dual-specificity kinase and establishes a previously unexplored paradigm for the self-regulation of biological signaling processes.

SUBMITTER: Heizmann B 

PROVIDER: S-EPMC2972992 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor.

Heizmann Beate B   Reth Michael M   Infantino Simona S  

Proceedings of the National Academy of Sciences of the United States of America 20101012 43


Upon B-cell activation, the signaling subunits Ig-α and Ig-β of the B-cell antigen receptor become phosphorylated not only on tyrosines but also on serine residues. Using a specific antibody, we show that serine 197 (S197) in the cytoplasmic tail of Ig-α is phosphorylated upon B-cell antigen receptor activation, and that this modification inhibits the signal output of the B-cell antigen receptor. Surprisingly, we found that the well-known protein tyrosine kinase Syk (spleen tyrosine kinase) phos  ...[more]

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