Structural Basis for Protein Phosphatase 1 Regulation and Specificity

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Catalytic Domain*
  • Holoenzymes / chemistry
  • Holoenzymes / metabolism
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism
  • Models, Molecular
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / metabolism
  • Protein Binding
  • Protein Phosphatase 1 / chemistry*
  • Protein Phosphatase 1 / metabolism
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism
  • Substrate Specificity

Substances

  • Holoenzymes
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • Protein Subunits
  • neurabin
  • Protein Phosphatase 1