BLNK: a central linker protein in B cell activation
BLNK: a central linker protein in B cell activation
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DOI：
10.1016/s1074-7613(00)80591-9
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发表时间：
1998-07-01
期刊：
影响因子：
32.4
通讯作者：
Chan, AC
中科院分区：
文献类型：
--
作者：
Fu, C;Turck, CW;Chan, AC
接头或衔接蛋白提供受体可以扩增和调节下游效应蛋白的机制。我们在此描述了一种新的（B）在bar ir蛋白下的bar细胞（1）下的鉴定，称为BLNK，其将B细胞受体相关的Syk酪氨酸激酶与PLC γ、Vav鸟嘌呤核苷酸交换因子以及Grb 2和Nck衔接蛋白连接。Syk对BLNK的酪氨酸磷酸化为这些含SH 2的效应分子提供了对接位点，这反过来又允许它们各自的信号传导途径的磷酸化和/或活化。因此，BLNK代表了一种中心连接蛋白，它将B细胞受体相关激酶与多种信号通路连接起来，并可能调节B细胞功能和发育的生物学结果。
Linker or adapter proteins provide mechanisms by which receptors can amplify and regulate downstream effector proteins. We describe here the identification of a novel (B) under bar cell (l) under bar ir protein, termed BLNK, that interfaces the B cell receptor-associated Syk tyrosine kinase with PLC gamma, the Vav guanine nucleotide exchange factor, and the Grb2 and Nck adapter proteins. Tyrosine phosphorylation of BLNK by Syk provides docking sites for these SH2-containing effector molecules that, in turn, permits the phosphorylation and/or activation of their respective signaling pathways. Hence, BLNK represents a central linker protein that bridges the B cell receptor-associated kinases with a multitude of signaling pathways and may regulate the biologic outcomes of B cell function and development.