Hock, A.K., Vigneron, A.M., Carter, S., Ludwig, R.L. and Vousden, K.H. (2011) Regulation of p53 stability and function by the deubiquitinating enzyme USP42. EMBO Journal, 30(24), pp. 4921-4930. (doi: 10.1038/emboj.2011.419)
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Publisher's URL: http://dx.doi.org/10.1038/emboj.2011.419
Abstract
The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by the ubiquitin ligase MDM2. In this study, we have identified USP42 as a DUB that interacts with and deubiquitinates p53. USP42 forms a direct complex with p53 and controls level of ubiquitination during the early phase of the response to a range of stress signals. Although we do not find a clear role for USP42 in controlling either the basal or fully activated levels of p53, the function of USP42 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent cell-cycle arrest in response to stress. These functions of USP42 are likely to contribute to the repair and recovery of cells from mild or transient damage.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Vousden, Karen |
Authors: | Hock, A.K., Vigneron, A.M., Carter, S., Ludwig, R.L., and Vousden, K.H. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
Journal Name: | EMBO Journal |
ISSN: | 0261-4189 |
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