Syk and pTyr'd: Signaling through the B cell antigen receptor

被引：134

作者：

Geahlen, Robert L. ^{[1
]}

机构：

[1] Purdue Univ, Dept Med Chem & Mol Pharmacol, W Lafayette, IN 47907 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2009年 / 1793卷 / 07期

关键词：

Syk; B cell activation; Antigen receptor; Protein-tyrosine kinase; Protein phosphorylation; Signal transduction; PROTEIN-TYROSINE KINASE; FC-EPSILON-RI; SRC HOMOLOGY-2 DOMAIN; ACTIVATION LOOP PHOSPHORYLATION; LINKER REGION TYROSINES; VAV BINDING-SITE; C-GAMMA; T-CELL; NEGATIVE REGULATION; STRUCTURAL BASIS;

D O I：

10.1016/j.bbamcr.2009.03.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The B cell receptor (BCR) transduces antigen binding into alterations in the activity of intracellular signaling pathways through its ability to recruit and activate the cytoplasmic protein-tyrosine kinase Syk. The recruitment of Syk to the receptor, its activation and its subsequent interactions with downstream effectors are all regulated by its phosphorylation on tyrosine. This review discusses our current understanding of how this phosphorylation regulates the activity of Syk and its participation in signaling through the BCR. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：1115 / 1127

页数：13

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