施一公《Cell》发表综述

　　

生物通报道，清华大学生命科学院结构生物学中心施一公日前在最新一期的Cell杂志上发表综述文章Serine/Threonine Phosphatases: Mechanism through Structure。

 

磷酸化是表观遗传学中的一个重要研究课题。我们知道，磷酸化是通过激酶和磷酸酶相对的活性来控制的，也正因此，磷酸化是一个可逆的过程。

 

特异的去磷酸化作用由少量的丝氨酸-苏氨酸磷酸酶蛋白（PSPs）控制，而这些蛋白又由上千个的磷蛋白亚基构成。很多的PSPs，比如说，磷酸酶1（PP1）和PP2A，通过保守的催化亚基单位和大量的调节性亚单位来达到识别特异底物和发挥调控作用的目的。其他的PSPs，以PP2C和FCP/SCP为代表，包含催化控制区和调节区。

 

在本综述中，施一公主要解析这些经典的PSPs的结构以及生化功能的关联，尤其以PP2A为重点介绍对象。

（生物通 小茜）

生物通推荐原文摘要

Serine/Threonine Phosphatases: Mechanism through Structure

Yigong Shi1, , 

1 Center for Structural Biology, School of Life Sciences, and School of Medicine, Tsinghua University, Beijing 100084, China

 

Corresponding author

 

【Summary】

The reversible phosphorylation of proteins is accomplished by opposing activities of kinases and phosphatases. Relatively few protein serine/threonine phosphatases (PSPs) control the specific dephosphorylation of thousands of phosphoprotein substrates. Many PSPs, exemplified by protein phosphatase 1 (PP1) and PP2A, achieve substrate specificity and regulation through combinatorial interactions between conserved catalytic subunits and a large number of regulatory subunits. Other PSPs, represented by PP2C and FCP/SCP, contain both catalytic and regulatory domains within the same polypeptide chain. Here, we discuss biochemical and structural investigations that advance the mechanistic understanding of the three major classes of PSPs, with a focus on PP2A.