Controlling Ser/Thr protein phosphatase PP1 activity and function through interaction with regulatory subunits

Adv Protein Chem Struct Biol. 2020:122:231-288. doi: 10.1016/bs.apcsb.2020.06.004. Epub 2020 Jul 25.

Abstract

Protein phosphatase 1 is a major Ser/Thr protein phosphatase activity in eukaryotic cells. It is composed of a catalytic polypeptide (PP1C), with little substrate specificity, that interacts with a large variety of proteins of diverse structure (regulatory subunits). The diversity of holoenzymes that can be formed explain the multiplicity of cellular functions under the control of this phosphatase. In quite a few cases, regulatory subunits have an inhibitory role, downregulating the activity of the phosphatase. In this chapter we shall introduce PP1C and review the most relevant families of PP1C regulatory subunits, with particular emphasis in describing the structural basis for their interaction.

Keywords: Enzyme inhibition; Protein phosphatases; Protein-protein interaction; Regulatory subunits; Targeting subunits.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Protein Phosphatase 1 / chemistry*
  • Protein Phosphatase 1 / metabolism*
  • Serine / chemistry
  • Serine / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity
  • Threonine / chemistry
  • Threonine / metabolism

Substances

  • Threonine
  • Serine
  • Protein Phosphatase 1