, Volume 51, Issue 6, pp 487-494
Date: 17 May 2008

Recent progress on the structure of Ser/Thr protein phosphatases

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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.

Supported by the National Basic Research Program of China (973) (Grant No 2004CB719906), and the National Natural Science Foundation of China (30470393)