FOCAL ADHESION KINASE: EXPLORING FAK STRUCTURE TO GAIN INSIGHT INTO FUNCTION

被引：101

作者：

Hall, Jessica E. ^{[1
]}

Fu, Wei ^{[1
]}

Schaller, Michael D. ^{[1
,2
,3
]}

机构：

[1] W Virginia Univ, Dept Biochem, Sch Med, Morgantown, WV 26506 USA

[2] W Virginia Univ, Mary Babb Randolph Canc Ctr, Sch Med, Morgantown, WV 26506 USA

[3] W Virginia Univ, Ctr Cardiovasc & Resp Sci, Sch Med, Morgantown, WV 26506 USA

来源：

INTERNATIONAL REVIEW OF CELL AND MOLECULAR BIOLOGY, VOL 288 | 2011年 / 288卷

关键词：

FAK; Domain structure; FERM; Kinase; FAT domain; Autoinhibition; Therapeutics; PROTEIN-TYROSINE KINASE; EPITHELIAL-SPECIFIC DISRUPTION; GROWTH-FACTOR RECEPTOR-3; PAXILLIN LD MOTIFS; N-TERMINAL DOMAIN; FACTOR-I RECEPTOR; FERM DOMAIN; SURVIVAL SIGNALS; TARGETING DOMAIN; CRYSTAL-STRUCTURES;

D O I：

10.1016/B978-0-12-386041-5.00005-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Focal adhesion kinase (FAK) and proline-rich tyrosine kinase 2 (Pyk2) are closely related nonreceptor protein tyrosine kinases. FAK can regulate cell proliferation, survival, and motility, and plays an essential role in development. Pyk2 shares some functions with FAK but is a nonessential gene product during development. Recent discoveries related to FAK and Pyk2 structure have provided important insights into the regulatory mechanisms of catalytic activity, molecular basis of assembly of signaling complexes, and the transmission of downstream signals. This chapter reviews these advances in FAK/Pyk2 structure/function, compares and contrasts features of these kinases, and discusses new drug discoveries in the context of molecular structure.

引用

页码：185 / 225

页数：41

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