| First Author | Heizmann B | Year | 2010 |
| Journal | Proc Natl Acad Sci U S A | Volume | 107 |
| Issue | 43 | Pages | 18563-8 |
| PubMed ID | 20940318 | Mgi Jnum | J:165501 |
| Mgi Id | MGI:4837577 | Doi | 10.1073/pnas.1009048107 |
| Citation | Heizmann B, et al. (2010) Syk is a dual-specificity kinase that self-regulates the signal output from the B-cell antigen receptor. Proc Natl Acad Sci U S A 107(43):18563-8 |
| abstractText | Upon B-cell activation, the signaling subunits Ig-alpha and Ig-beta 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-alpha 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-alpha, 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. |
