Structural basis for protein phosphatase 1 regulation and specificity

被引:196
作者
Peti, Wolfgang [1 ,2 ]
Nairn, Angus C. [3 ]
Page, Rebecca [4 ]
机构
[1] Brown Univ, Dept Mol Pharmacol Physiol & Biotechnol, Providence, RI 02912 USA
[2] Brown Univ, Dept Chem, Providence, RI 02912 USA
[3] Yale Univ, Sch Med, Dept Psychiat, New Haven, CT USA
[4] Brown Univ, Dept Mol Biol Cell Biol & Biochem, Providence, RI 02912 USA
基金
美国国家科学基金会;
关键词
enzyme regulation; enzyme specificity; protein phosphatase 1; structural biology; INTRINSICALLY UNSTRUCTURED PROTEINS; CATALYTIC SUBUNIT; CRYSTAL-STRUCTURE; HUMAN CALCINEURIN; DOCKING MOTIF; SPINOPHILIN; COMPLEX; BINDING; INHIBITOR-2; IDENTIFICATION;
D O I
10.1111/j.1742-4658.2012.08509.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ubiquitous serine/threonine protein phosphatase 1 (PP1) regulates diverse, essential cellular processes such as cell cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling. However, the free catalytic subunit of PP1, while an effective enzyme, lacks substrate specificity. Instead, it depends on a diverse set of regulatory proteins (= 200) to confer specificity towards distinct substrates. Here, we discuss recent advances in structural studies of PP1 holoenzyme complexes and summarize the new insights these studies have provided into the molecular basis of PP1 regulation and specificity.
引用
收藏
页码:596 / 611
页数:16
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