title: Dubble or nothing? Is HAUSP deubiquitylating enzyme the final arbiter of p53 levels?
abstract: 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.
authors.affiliation: 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
authors.forename: Stephen A
authors.initials: SA
authors.lastname: Wood
mesh_terms: 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
chemical_list: 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