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Structural Basis for Protein Phosphatase 1 Regulation and Specificity

阿平添加于 2012-2-1 17:09 | 1612 次阅读 | 0 个评论

作者
Peti W, Nairn AC, Page R
摘要
The ubiquitous Ser/Thr 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.
详细资料
- 文献种类: Journal Article
- 期刊名称: The FEBS Journal
- 期刊缩写: FEBS J
- 期卷页: 2012年
- 地址: Department of Molecular Pharmacology, Physiology and Biotechnology Department of Chemistry, Brown University, Providence, RI 02912, USA Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06508, USA Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, RI 02912, USA
- ISBN: 1742-464X
学科领域生物医药 » 生物学
标签

PP1
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Structural Basis for Protein Phosphatase 1 Regulation and Specificity
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