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FERM Domain Interaction Promotes FAK Signaling

机译：FERM域交互促进FAK信令

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摘要

From the results of deletion analyses, the FERM domain of FAK has been proposed to inhibit enzymatic activity and repress FAK signaling. We have identified a sequence in the FERM domain that is important for FAK signaling in vivo. Point mutations in this sequence had little effect upon catalytic activity in vitro. However, the mutant exhibits reduced tyrosine phosphorylation and dramatically reduced Src family kinase binding. Further, the abilities of the mutant to transduce biochemical signals and to promote cell migration were severely impaired. The results implicate a FERM domain interaction in cell adhesion-dependent activation of FAK and downstream signaling. We also show that the purified FERM domain of FAK interacts with full-length FAK in vitro, and mutation of this sequence disrupts the interaction. These findings are discussed in the context of models of FAK regulation by its FERM domain.
机译：根据缺失分析的结果，已提出FAK的FERM结构域抑制酶活性并抑制FAK信号传导。我们已经在FERM域中鉴定了一个序列，该序列对于体内FAK信号传导很重要。该序列中的点突变对体外催化活性影响很小。但是，该突变体表现出减少的酪氨酸磷酸化和显着减少的Src家族激酶结合。此外，该突变体转导生化信号和促进细胞迁移的能力严重受损。结果暗示FERM域相互作用在FAK和下游信号传导的细胞粘附依赖性激活中。我们还显示纯化的FAK的FERM域与体外的全长FAK相互作用，并且此序列的突变会破坏相互作用。在FAK对其FERM域进行FAK调控的模型中讨论了这些发现。

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