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整合素、踝蛋白和纽带蛋白的尾部。

The tail of integrins, talin, and kindlins.

作者信息

Moser Markus, Legate Kyle R, Zent Roy, Fässler Reinhard

机构信息

Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.

出版信息

Science. 2009 May 15;324(5929):895-9. doi: 10.1126/science.1163865.

Abstract

Integrins are transmembrane cell-adhesion molecules that carry signals from the outside to the inside of the cell and vice versa. Like other cell surface receptors, integrins signal in response to ligand binding; however, events within the cell can also regulate the affinity of integrins for ligands. This feature is important in physiological situations such as those in blood, in which cells are always in close proximity to their ligands, yet cell-ligand interactions occur only after integrin activation in response to specific external cues. This review focuses on the mechanisms whereby two key proteins, talin and the kindlins, regulate integrin activation by binding the tails of integrin-beta subunits.

摘要

整合素是跨膜细胞粘附分子,可将信号从细胞外部传递到内部,反之亦然。与其他细胞表面受体一样,整合素在配体结合时发出信号;然而,细胞内的事件也可以调节整合素对配体的亲和力。这一特性在诸如血液中的生理情况下很重要,在血液中细胞总是与其配体紧密相邻,但细胞-配体相互作用仅在整合素响应特定外部信号被激活后才会发生。本综述重点关注两种关键蛋白——踝蛋白和纽带蛋白——通过结合整合素β亚基的尾部来调节整合素激活的机制。

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