Changing venues for tumour suppression: balancing destruction and localization by monoubiquitylation

Nat Rev Cancer. 2007 Jun;7(6):409-13. doi: 10.1038/nrc2145. Epub 2007 May 17.


Recent studies have shown that three major tumour-suppressor proteins undergo monoubiquitylation-mediated nuclear-cytoplasmic shuttling. Importantly, this mechanism has consequences for cancer and implies that proper localization is central to the function of tumour suppressors. This Progress article highlights recent efforts demonstrating that monoubiquitylation coupled to nuclear-cytoplasmic shuttling might be a novel regulatory mechanism that directly influences the function of tumour suppressors.

Publication types

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

MeSH terms

  • Active Transport, Cell Nucleus
  • Cytoplasm / metabolism
  • Forkhead Transcription Factors / metabolism
  • Humans
  • Models, Biological
  • Oxidative Stress
  • PTEN Phosphohydrolase / metabolism
  • Tumor Suppressor Proteins / metabolism*
  • Ubiquitin / metabolism*
  • Ubiquitin-Protein Ligases / metabolism*


  • Forkhead Transcription Factors
  • Tumor Suppressor Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • PTEN Phosphohydrolase
  • PTEN protein, human