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FEBS J. 2013 Jan;280(2):596-611. doi: 10.1111/j.1742-4658.2012.08509.x. Epub 2012 Feb 24.

Structural basis for protein phosphatase 1 regulation and specificity.

Author information

1
Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, RI 02912, USA. wolfgang_peti@brown.edu

Abstract

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.

PMID:
22284538
PMCID:
PMC3350600
DOI:
10.1111/j.1742-4658.2012.08509.x
[Indexed for MEDLINE]
Free PMC Article

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