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

Leonardo Salmena; Pier Paolo Pandolfi

doi:10.1038/nrc2145

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.

Authors

Leonardo Salmena¹, Pier Paolo Pandolfi

Affiliation

¹ Cancer Biology and Genetics Program and Department of Pathology, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.

PMID: 17508027
DOI: 10.1038/nrc2145

Abstract

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*

Substances

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