Changing venues for tumour suppression: balancing destruction and localization by monoubiquitylation.
review · Level V
Where this comes from
- Record sourced from PubMed, PMID 17508027.
- Also identified by DOI 10.1038/nrc2145.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.
Medical subject headings
- Tumor Suppressor Proteins
- Ubiquitin
- Ubiquitin-Protein Ligases