How ILK and kindlins cooperate to orchestrate integrin signaling
How ILK and kindlins cooperate to orchestrate integrin signaling
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DOI：
10.1016/j.ceb.2009.05.008
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发表时间：
2009-10-01
影响因子：
7.5
通讯作者：
Faessler, Reinhard
中科院分区：
文献类型：
--
作者：
Boettcher, Ralph T.;Lange, Anika;Faessler, Reinhard
整合素介导的细胞粘附调节对发育、生理学和病理学至关重要的多种细胞过程。由于整联蛋白缺乏酶活性，它们需要募集衔接蛋白和信号蛋白来介导它们的功能。细胞质蛋白质Kindlin和整合素连接激酶（ILK）与整合素尾部缔合，从而将整合素与肌动蛋白细胞骨架和各种信号传导途径连接。与它们在调节细胞-基质粘附中的整合素功能中的作用相比，对Kindlin和ILK在其他细胞隔室（例如细胞-细胞接触和细胞核中）中的功能知之甚少。
Integrin-mediated cell adhesion regulates multiple cellular processes crucial for development, physiology, and pathology. Since integrins lack enzymatic activity they need to recruit adaptor and signaling proteins to mediate their functions. The cytoplasmic proteins kindlins and integrin-linked kinase (ILK) associate with integrin tails and thereby link integrins with the actin cytoskeleton and various signaling pathways. In comparison to their role in regulating integrin function in cell-matrix adhesions, less is known about the functions of kindlins and ILK in other cellular compartments, such as cell-cell contacts and in the nucleus.