The PTEN protein: cellular localization and post-translational regulation

Biochem Soc Trans. 2016 Feb;44(1):273-8. doi: 10.1042/BST20150224.

Abstract

The phosphatase and tensin homologue deleted on chromosome 10 (PTEN) phosphatase dephosphorylates PIP3, the lipid product of the class I PI 3-kinases, and suppresses the growth and proliferation of many cell types. It has been heavily studied, in large part due to its status as a tumour suppressor, the loss of function of which is observed through diverse mechanisms in many tumour types. Here we present a concise review of our understanding of the PTEN protein and highlight recent advances, particularly in our understanding of its localization and regulation by ubiquitination and SUMOylation.

Keywords: AKT; cancer; phosphatase; phosphoinositide 3-kinase; signal transduction; ubiquitin.

Publication types

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

MeSH terms

  • Cells / enzymology*
  • Humans
  • PTEN Phosphohydrolase / metabolism*
  • Protein Processing, Post-Translational*
  • Protein Transport
  • Small Ubiquitin-Related Modifier Proteins / metabolism
  • Ubiquitin / metabolism

Substances

  • Small Ubiquitin-Related Modifier Proteins
  • Ubiquitin
  • PTEN Phosphohydrolase