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

被引：41

作者：

Heizmann, Beate ^{[1
,2
]}

Reth, Michael ^{[1
,2
]}

Infantino, Simona ^{[1
,2
]}

机构：

[1] Univ Freiburg, BIOSS, Ctr Biol Signalling Studies, D-79104 Freiburg, Germany

[2] Max Planck Inst Immunobiol, D-79108 Freiburg, Germany

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 43期

基金：

瑞士国家科学基金会;

关键词：

PROTEIN-TYROSINE KINASE; PHOSPHORYLATED ITAM PEPTIDE; PHOSPHOINOSITIDE; 3-KINASE; SERINE PHOSPHORYLATION; ACTIVATION; TRANSDUCTION; PURIFICATION; LYMPHOCYTES; EXPRESSION; ANTIBODIES;

D O I：

10.1073/pnas.1009048107

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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-a 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.

引用

页码：18563 / 18568

页数：6

共 39 条

[1] SYK is upstream of phosphoinositide 3-kinase in B cell receptor signaling [J].