Recent progress on the structure of Ser/Thr protein phosphatases
PP1, PP2A and PP2B, belonging to the PPP family of Ser/Thr protein phosphatases, participate in regulating many important physiological processes, such as cell cycle control, regulation of cell growth and division regulation, etc. The sequence homology between them is relatively high, and tertiary structure is conserved. Because of the complexity of the structure of PP2A and the diversity of its regulatory subunits, its structure is less well known than those of PP1 and PP2B. The PP2A holoenzyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic subunit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phsphatases structures are summarized.
KeywordsSer/Thr phosphatases subunit composition similarities and differences crystal structure
Unable to display preview. Download preview PDF.
- 1.Toole B J, Cohen P T. The skeletal muscle-specific glycogen-targeted protein phosphatase 1 plays a major role in the regulation of glycogen metabolism by adrenaline in vivo. Cell Signal, 2007, 19(5): 1044–1055, 17257813, 10.1016/j.cellsig.2006.11.013, 1:CAS:528:DC%2BD2sXjsVSru7w%3DCrossRefGoogle Scholar
- 5.Andreassen P R, Lacroix F B, Moruzzi V E, et al. Differential subcellular localization of protein phosphatase-1 alpha, gammal and delta isoforms during both interphase and mitosis in mammalian cells. J Cell Biol, 1998, 141(5): 1207–1215, 9606212, 10.1083/jcb.141.5.1207, 1:CAS:528:DyaK1cXjs12ntLc%3DCrossRefGoogle Scholar
- 8.Rusnak F, Mertz P. Calcineurin: Form and function. Physiological Rev, 2000, 80(4): 1483–1521, 1:CAS:528:DC%2BD3cXnsVKisLk%3DGoogle Scholar
- 10.Cho U S, Xu W Q. Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature, 2006, 445(1): 53–57, 17086192, 10.1038/nature05351Google Scholar
- 15.Xie X J, Huang W, Xue C Z, et al. The β12–β13 loop is a key regulatory element for activity and property in the catalytic domain of protein phosphatase 1 and 2B. Biol Chem, 2006, 387(10): 1461–1467, 17081120, 10.1515/BC.2006.183, 1:CAS:528:DC%2BD28XhtFygtLnEGoogle Scholar
- 16.Maynes J T, Luu H A, Cherney M M, et al. Crystal structure of protein phosphatase-1 bound to Motuporin and Dihydromicrocystin-LA: Elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins. J Mol Biol, 2006, 356(10): 111–120, 16343532, 10.1016/j.jmb.2005.11.019, 1:CAS:528:DC%2BD28XjvVOguw%3D%3DCrossRefGoogle Scholar
- 21.Qing H, Kim H Y, Liu Y D, et al. Crystal structure of calcineurincyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes. Proc Natl Acad Sci USA, 2002, 99(17): 12037–12042Google Scholar
- 26.Tokoyoda K, Takemoto Y, Nakayama T, et al. Synergism between the calmodulin-binding and autoinhibitory domains on calcineurin is essential for the induction of their phosphatase activity. J Biol Chem, 2000, 275(16): 11728–11735, 10766794, 10.1074/jbc.275.16.11728, 1:CAS:528:DC%2BD3cXisl2jsrY%3DCrossRefGoogle Scholar
- 31.Shenolikar S, Nairn A C. Protein phosphatases: Recent progress. Adv Second Messenger Phosphoprotein Res, 1991, 23: 1–121, 1847640, 1:STN:280:By6C2cvovFM%3DGoogle Scholar