How focal adhesion kinase achieves regulation by linking ligand binding, localization and action

被引：58

作者：

Arold, Stefan T. ^{[1
]}

机构：

[1] Univ Texas MD Anderson Canc Ctr, Dept Biochem & Mol Biol, Unit 1000, Houston, TX 77030 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2011年 / 21卷 / 06期

基金：

美国国家卫生研究院;

关键词：

STRUCTURAL BASIS; FAK PHOSPHORYLATION; DOMAIN; REQUIREMENT; INSIGHT; COMPLEX; MECHANISMS; EXPRESSION; DYNAMICS; REVEALS;

D O I：

10.1016/j.sbi.2011.09.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Focal adhesion kinase (FAK) has an astonishing number of ligands and functions, which enable it to contribute to embryonic development and human health. FAK can promote different effects in similar cellular environments or similar effects in different cellular environments. Recent advances in structural and cellular analysis of FAK are starting to reveal the interrelationships between the conformations, localizations, interactions, and functions of FAK. This review focuses on our emerging understanding of how the structural framework of FAK mechanistically allows it to integrate manifold stimuli into environment-specific functions.

引用

页码：808 / 813

页数：6

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