Changing venues for tumour suppression: balancing destruction and localization by monoubiquitylation.
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.
Salmena
Leonardo
L
Cancer Biology and Genetics Program and Department of Pathology, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
Pandolfi
Pier Paolo
PP
D021581:Active Transport, Cell Nucleus; D003593:Cytoplasm / Q000378:metabolism; D051858:Forkhead Transcription Factors / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D018384:Oxidative Stress; D051059:PTEN Phosphohydrolase / Q000378:metabolism; D025521:Tumor Suppressor Proteins / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D051858:Forkhead Transcription Factors; D025521:Tumor Suppressor Proteins; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases; D051059:PTEN Phosphohydrolase; C494929:PTEN protein, human