Department of Biochemistry, West Virginia University School of Medicine, Morgantown, West Virginia, USA.
Int Rev Cell Mol Biol. 2011;288:185-225. doi: 10.1016/B978-0-12-386041-5.00005-4.
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.
黏着斑激酶（FAK）和富含脯氨酸的酪氨酸激酶 2（Pyk2）是密切相关的非受体酪氨酸激酶。FAK 可以调节细胞增殖、存活和迁移，在发育中起着重要作用。Pyk2 与 FAK 具有一些相同的功能，但在发育过程中是非必需的基因产物。最近与 FAK 和 Pyk2 结构相关的发现为催化活性的调节机制、信号复合物组装的分子基础以及下游信号的传递提供了重要的见解。本章综述了 FAK/Pyk2 结构/功能方面的这些进展，比较和对比了这些激酶的特点，并讨论了分子结构背景下的新药发现。
