Cutting edge: association of phospholipase C-gamma 2 Src homology 2 domains with BLNK is critical for B cell antigen receptor signaling.
Cutting edge: association of phospholipase C-gamma 2 Src homology 2 domains with BLNK is critical for B cell antigen receptor signaling.
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最前沿：磷脂酶 C-gamma 2 Src 同源 2 结构域与 BLNK 的关联对于 B 细胞抗原受体信号转导至关重要。
作者：
M. Ishiai;Hitoshi Sugawara;M. Kurosaki;T. Kurosaki
为了探讨磷脂酶C(PLC)-γ2参与B细胞抗原受体(BCR)信号转导的机制(S)，我们研究了PLC-γ2突变体在缺失PLC-γ2的B细胞中的作用。对SH2(N)需求的一个可能的解释是，该突变取消了PLC-Gamma 2与接头蛋白BLNK的关联。此外，表达带有SH2(N)突变的膜相关形式(CD16/PLC-Gamma 2)需要将BCR和CD16连接以产生1，4，5-三磷酸肌醇。综上所述，我们的结果表明，SH2(N)结构域通过与BLNK结合，引导PLC-Gamma 2进入BCR信号复合体的邻近区域，从而使PLC-Gamma 2酪氨酸磷酸化，从而激活PLC-Gamma 2。
To explore the mechanism(s) by which phospholipase C (PLC)-gamma 2 participates in B cell Ag receptor (BCR) signaling, we have studied the function of PLC-gamma 2 mutants in B cells deficient in PLC-gamma 2. Mutation of the N-terminal Src homology 2 domain [SH2(N)] resulted in the complete loss of inositol 1,4, 5-trisphosphate generation upon BCR engagement. A possible explanation for the SH2(N) requirement was provided by findings that this mutation abrogates the association of PLC-gamma 2 with an adaptor protein BLNK. Moreover, expression of a membrane-associated form (CD16/PLC-gamma 2) with SH2(N) mutation required coligation of BCR and CD16 for inositol 1,4,5-trisphosphate generation. Together, our results suggest a central role for the SH2(N) domain in directing PLC-gamma 2 into the close proximity of BCR signaling complex by its association with BLNK, whereby PLC-gamma 2 becomes tyrosine phosphorylated and thereby activated.
DOI：
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影响因子：
32.4
作者：
Fu, C;Turck, CW;Chan, AC
通讯作者：
Chan, AC
鼠 B 淋巴细胞表达磷脂酶 C 同工酶。
DOI：
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发表时间：
1991
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
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作者：
Hempel,WM;DeFranco,AL
通讯作者：
DeFranco,AL