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

Antonio Casamayor, Joaquín Ariño*

*Corresponding author for this work

Research output: Contribution to journalReview articleResearchpeer-review

11 Citations (Scopus)

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.

Original languageAmerican English
Pages (from-to)231-288
Number of pages58
JournalAdvances in Protein Chemistry and Structural Biology
Volume122
DOIs
Publication statusPublished - 1 Jan 2020

Keywords

  • Enzyme inhibition
  • Protein phosphatases
  • Protein-protein interaction
  • Regulatory subunits
  • Targeting subunits

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