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首页> 外文期刊>Molecular and Cellular Biology >Src SH2 Arginine 175 Is Required for Cell Motility: Specific Focal Adhesion Kinase Targeting and Focal Adhesion Assembly Function
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Src SH2 Arginine 175 Is Required for Cell Motility: Specific Focal Adhesion Kinase Targeting and Focal Adhesion Assembly Function

机译：Src SH2精氨酸175是细胞运动所必需的：特定的黏着斑激酶定位和黏着斑组装功能

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摘要

Src kinase is a crucial mediator of adhesion-related signaling and motility. Src binds to focal adhesion kinase (FAK) through its SH2 domain and subsequently activates it for phosphorylation of downstream substrates. In addition to this binding function, data suggested that the SH2 domain might also perform an important role in targeting Src to focal adhesions (FAs) to enable further substrate phosphorylations. To examine this, we engineered an R175L mutation in cSrc to prevent the interaction with FAK pY397. This constitutively open Src kinase mediated up-regulated substrate phosphorylation in SYF cells but was unable to promote malignant transformation. Significantly, SrcR175L cells also had a profound motility defect and an impaired FA generation capacity. Importantly, we were able to recapitulate wild-type motile behavior and FA formation by directing the kinase to FAs, clearly implicating the SH2 domain in recruitment to FAK and indicating that this targeting capacity, and not simply Src-FAK scaffolding, was critical for normal Src function.
机译：Src激酶是粘附相关信号和运动的关键介质。 Src通过其SH2结构域与粘着斑激酶（FAK）结合，并随后激活它以使下游底物磷酸化。除此结合功能外，数据表明，SH2结构域在将Src靶向粘着斑（FA）以实现进一步的底物磷酸化方面也可能起重要作用。为了检查这一点，我们在cSrc中设计了一个R175L突变，以防止与FAK pY397的相互作用。这种组成性开放Src激酶介导SYF细胞中底物磷酸化的上调，但不能促进恶性转化。重要的是，SrcR175L细胞还具有严重的运动缺陷和FA生成能力受损。重要的是，我们能够通过将激酶引导至FA来概括野生型运动行为和FA的形成，明确暗示SH2结构域募集到FAK中，并表明这种靶向能力（而不仅仅是Src-FAK支架）对于正常人至关重要Src功能。

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