Dubble or nothing? Is HAUSP deubiquitylating enzyme the final arbiter of p53 levels?
Related Experiment Video
Updated: Aug 6, 2026

Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
Published on: May 10, 2015
1Child 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
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.
Related Concept Videos
Negative Regulator Molecules
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
DNA Damage can Stall the Cell Cycle
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Abnormal Proliferation
DNA Damage Can Stall the Cell Cycle

