Shi Yigong
Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Cell. 2009 Oct 30;139(3):468-84. doi: 10.1016/j.cell.2009.10.006.
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.
蛋白质的可逆磷酸化是通过激酶和磷酸酶的相反活性来完成的。相对较少的蛋白质丝氨酸/苏氨酸磷酸酶（PSP）控制着数千种磷酸化蛋白底物的特异性去磷酸化。许多PSP，如蛋白磷酸酶1（PP1）和PP2A，通过保守催化亚基和大量调节亚基之间的组合相互作用来实现底物特异性和调节。其他PSP，以PP2C和FCP/SCP为代表，在同一多肽链中同时包含催化和调节结构域。在这里，我们讨论了有助于深入理解三大类PSP作用机制的生化和结构研究，重点是PP2A。
