The human phosphatase interactome: An intricate family portrait

FEBS Lett. 2012 Aug 14;586(17):2732-9. doi: 10.1016/j.febslet.2012.05.008. Epub 2012 May 21.

Abstract

The concerted activities of kinases and phosphatases modulate the phosphorylation levels of proteins, lipids and carbohydrates in eukaryotic cells. Despite considerable effort, we are still missing a holistic picture representing, at a proteome level, the functional relationships between kinases, phosphatases and their substrates. Here we focus on phosphatases and we review and integrate the available information that helps to place the members of the protein phosphatase superfamilies into the human protein interaction network. In addition we show how protein interaction domains and motifs, either covalently linked to the phosphatase domain or in regulatory/adaptor subunits, play a prominent role in substrate selection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Binding Sites
  • Catalytic Domain
  • Humans
  • Peptides / chemistry
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / physiology
  • Phosphorylation
  • Phylogeny
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Tyrosine / chemistry

Substances

  • Peptides
  • Tyrosine
  • Phosphoric Monoester Hydrolases