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首页> 外文期刊>Molecular and Cellular Biology >Functional Independence and Interdependence of the Src Homology Domains of Phospholipase C-γ1 in B-Cell Receptor Signal Transduction
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Functional Independence and Interdependence of the Src Homology Domains of Phospholipase C-γ1 in B-Cell Receptor Signal Transduction

机译：B细胞受体信号转导中磷脂酶C-γ1的Src同源域的功能独立性和相互依赖性

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摘要

B-cell receptor (BCR)-induced activation of phospholipase C-γ1 (PLCγ1) and PLCγ2 is crucial for B-cell function. While several signaling molecules have been implicated in PLCγ activation, the mechanism coupling PLCγ to the BCR remains undefined. The role of PLCγ1 SH2 and SH3 domains at different steps of BCR-induced PLCγ1 activation was examined by reconstitution in a PLCγ-negative B-cell line. PLCγ1 membrane translocation required a functional SH2 N-terminal [SH2(N)] domain, was decreased by mutation of the SH3 domain, but was unaffected by mutation of the SH2(C) domain. Tyrosine phosphorylation did not require the SH2(C) or SH3 domains but depended exclusively on a functional SH2(N) domain, which mediated the association of PLCγ1 with the adapter protein, BLNK. Forcing PLCγ1 to the membrane via a myristoylation signal did not bypass the SH2(N) domain requirement for phosphorylation, indicating that the phosphorylation mediated by this domain is not due to membrane anchoring alone. Mutation of the SH2(N) or the SH2(C) domain abrogated BCR-stimulated phosphoinositide hydrolysis and signaling events, while mutation of the SH3 domain partially decreased signaling. PLCγ1 SH domains, therefore, have interrelated but distinct roles in BCR-induced PLCγ1 activation.
机译：B细胞受体（BCR）诱导的磷脂酶C-γ1（PLCγ1）和PLCγ2活化对于B细胞功能至关重要。尽管几个信号分子与PLCγ的激活有关，但将PLCγ耦合到BCR的机制仍然不确定。通过在PLCγ-阴性B细胞系中的重构，检查了PLCγ1SH2和SH3结构域在BCR诱导的PLCγ1活化的不同步骤中的作用。 PLCγ1膜易位需要一个功能性的SH2 N端[SH2（N）]域，通过SH3域的突变而减少，但不受SH2（C）域的突变的影响。酪氨酸磷酸化不需要SH2（C）或SH3域，但仅依赖于功能性SH2（N）域，后者介导PLCγ1与衔接蛋白BLNK的缔合。通过肉豆蔻酰化信号迫使PLCγ1进入膜并没有绕过SH2（N）结构域对磷酸化的要求，这表明由该结构域介导的磷酸化并非仅由于膜锚定。 SH2（N）或SH2（C）域的突变废除了BCR刺激的磷酸肌醇水解和信号转导事件，而SH3域的突变则部分降低了信号转导。因此，PLCγ1SH结构域在BCR诱导的PLCγ1激活中具有相互关联但又不同的作用。

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