Sci. STKE, 30 July 2002
Vol. 2002, Issue 143, p. pe34
[DOI: 10.1126/stke.2002.143.pe34]
PERSPECTIVES
Dubble or Nothing? Is HAUSP Deubiquitylating Enzyme the Final Arbiter of p53 Levels?
Stephen A. Wood*
Child Health Research Institute and Centre for the Molecular Genetics of Development, University of Adelaide, 72 King William Road, North Adelaide, 5006, Australia.
Summary:
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 ß-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.
*Contact information. E-mail: stephen.wood{at}adelaide.edu.au
Citation: S. A. Wood, Dubble or Nothing? Is HAUSP Deubiquitylating Enzyme the Final Arbiter of p53 Levels? Sci. STKE 2002, pe34 (2002).
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