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Sci. STKE, 30 July 2002
Vol. 2002, Issue 143, p. pe34
[DOI: 10.1126/scisignal.1432002pe34]

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.

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 β-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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