Proline-rich tyrosine kinase 2 and its inhibitor PRNK  

作　　者：Hao Jia Guo Hong You Kai Xiao Yinbing 

机构地区：[1]Cardiovascular Surgery Center, Xinqiao Hospital Third Military Medical University, Chongqing 400037, China

出　　处：《Journal of Medical Colleges of PLA(China)》2010年第5期307-312,共6页中国人民解放军军医大学学报（英文版）

基　　金：Supported by the National Natural Science Foundation of China(30700822)

摘　　要：Proline-rich tyrosine kinase 2 (Pyk2) is a nonreceptor protein tyrosine kinase,which is also known as Ca2 +-dependent tyrosine kinase or related adhesion focal tyrosine kinase.Pyk2 activation exerts a critical regulatory mechanism for various physiological processes including cytoskeleton function,regulation of cell growth and death,modulation of ion channels and multiple signaling events.However,mechanisms underlying the functional diversity of Pyk2 are not clear.A Pyk2 isoform that encodes only part of the C-terminal domain of Pyk2,named as PRNK (Pyk2-related non-kinase),acts as a dominant-negative inhibitor of Pyk2-dependent signaling by displacing Pyk2 from focal adhesions.Research on functional PRNK probably provides new potential inhibitory tool targeting Pyk2 and makes it possible to explore more of Pyk2 pathological mechanism.PRNK is a promising candidate targeting Pyk2 modulation.This review focuses on the functional investigation of Pyk2 and its structure and localization,including recent research with inhibitory strategies targeting Pyk2 by the method of PRNK.Proline-rich tyrosine kinase 2 （Pyk2） is a nonreceptor protein tyrosine kinase, which is also known as Ca2＋-dependent tyrosine kinase or related adhesion focal tyrosine kinase. Pyk2 activation exerts a critical regulatory mechanism for various physiological processes including cytoskeleton function, regulation of cell growth and death, modulation of ion channels and multiple signaling events. However, mechanisms underlying the functional diversity of Pyk2 are not clear. A Pyk2 isoform that encodes only part of the C-terminal domain of Pyk2, named as PRNK （Pyk2-related non-kinase）, acts as a dominant-negative inhibitor of Pyk2-dependent signaling by displacing Pyk2 from focal adhesions. Research on functional PRNK probably provides new potential inhibitory tool targeting Pyk2 and makes it possible to explore more of Pyk2 pathological mechanism. PRNK is a promising candidate targeting Pyk2 modulation. This review focuses on the functional investigation of Pyk2 and its structure and localization, including recent research with inhibitory strategies targeting Pyk2 by the method of PRNK.

关 键 词：Proline-rich tyrosine kinase 2 Pyk2 related non-kinase Dominant negative 

分 类 号：Q51[生物学—生物化学] TD923.14[矿业工程—选矿]