Changing venues for tumour suppression: Balancing destruction and localization by monoubiquitylation Journal Article


Authors: Salmena, L.; Pandolfi, P. P.
Article Title: Changing venues for tumour suppression: Balancing destruction and localization by monoubiquitylation
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. © 2007 Nature Publishing Group.
Keywords: review; cancer localization; ubiquitin; protein function; forkhead transcription factors; dna damage; dna repair; gene overexpression; apoptosis; models, biological; protein degradation; genetic transcription; protein p53; cancer inhibition; dna; protein processing; ubiquitination; molecular recognition; protein p27; tumor suppressor proteins; phosphatidylinositol 3,4,5 trisphosphate 3 phosphatase; pten phosphohydrolase; cytoplasm; active transport, cell nucleus; oxidative stress; ubiquitin protein ligase e3; cellular stress response; tumor suppressor protein; positive feedback; ubiquitin-protein ligases; apc protein; cancer cell destruction; protein mdm2; golgi complex; transcription factor foxo; protein p73
Journal Title: Nature Reviews Cancer
Volume: 7
Issue: 6
ISSN: 1474-175X
Publisher: Nature Publishing Group  
Date Published: 2007-06-01
Start Page: 409
End Page: 413
Language: English
DOI: 10.1038/nrc2145
PUBMED: 17508027
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 26" - "Export Date: 17 November 2011" - "CODEN: NRCAC" - "Source: Scopus"
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors