Dubble or nothing? Is HAUSP deubiquitylating enzyme the final arbiter of p53 levels?
Signal transduction processes can be regulated by biochemical modifications that affect protein activity or localization and by protein stability. Proteins implicated in cancer, such as beta-catenin and p53, are regulated by a combination of posttranslational modifications and protein degradation by the ubiquitin-proteasome pathway. Wood explores how ubiquitylation of these proteins may not be as unidirectional as previously thought. With the identification of substrate-specific deubiquitylating enzymes, ubiquitylation may not always lead to protein destruction, but may provide another finely tunable step for controlling protein activity.
Wood
Stephen A
SA
Child Health Research Institute and Centre for the Molecular Genetics of Development, University of Adelaide, 72 King William Road, North Adelaide, 5006, Australia. stephen.wood@adelaide.edu.au
D000818:Animals; D002352:Carrier Proteins / Q000502:physiology; D010450:Endopeptidases / Q000502:physiology*; D006801:Humans; D009687:Nuclear Proteins / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism* / Q000502:physiology; D025801:Ubiquitin / Q000378:metabolism* / Q000502:physiology; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7
D002352:Carrier Proteins; D009687:Nuclear Proteins; D016159:Tumor Suppressor Protein p53; D025801:Ubiquitin; D010450:Endopeptidases; C464569:USP7 protein, human; D043222:Ubiquitin Thiolesterase; D000076084:Ubiquitin-Specific Peptidase 7