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整合素连接激酶(ILK)和纽带蛋白如何协同调控整合素信号传导。

How ILK and kindlins cooperate to orchestrate integrin signaling.

作者信息

Böttcher Ralph T, Lange Anika, Fässler Reinhard

机构信息

Department of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.

出版信息

Curr Opin Cell Biol. 2009 Oct;21(5):670-5. doi: 10.1016/j.ceb.2009.05.008. Epub 2009 Jun 25.

Abstract

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.

摘要

整合素介导的细胞黏附调节着对发育、生理和病理至关重要的多种细胞过程。由于整合素缺乏酶活性,它们需要招募衔接蛋白和信号蛋白来介导其功能。胞质蛋白亲环蛋白和整合素连接激酶(ILK)与整合素尾部结合,从而将整合素与肌动蛋白细胞骨架和各种信号通路联系起来。与它们在调节细胞-基质黏附中整合素功能的作用相比,人们对亲环蛋白和ILK在其他细胞区室(如细胞-细胞接触和细胞核)中的功能了解较少。

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