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, 2010 Oct 26.
Article
em En
| MEDLINE
| ID: mdl-20940318
ABSTRACT
Upon B-cell activation, the signaling subunits Ig-α and Ig-ß 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) phosphorylates S197 on Ig-α, 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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Tirosina Quinases
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Linfócitos B
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Receptores de Antígenos de Linfócitos B
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Peptídeos e Proteínas de Sinalização Intracelular
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article