Abstract
Ubiquitination plays a key role in regulating the tumour suppressor p53. It targets p53 for degradation by the 26S proteasome. The ubiquitin pathway also regulates the activity and localisation of p53. Ubiquitination requires ubiquitin-activating and -conjugating enzymes and ubiquitin ligases. In addition, ubiquitination can be reversed by the action of deubiquitinating enzymes. Here we give an overview of the role of components of the ubiquitin-proteasome system in the regulation of p53 and review progress in targeting these proteins to activate wild-type p53 for the treatment of cancer. (C) 2009 Published by Elsevier Ltd.
| Original language | English |
|---|---|
| Pages (from-to) | 29-39 |
| Number of pages | 11 |
| Journal | Seminars in Cancer Biology |
| Volume | 20 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Feb 2010 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Ubiquitin
- P53
- Mdm2
- MdmX
- 26S proteasome
- E1
- E2
- E3
- Deubiquitinating enzyme
- SMALL-MOLECULE INHIBITORS
- EARLY EMBRYONIC LETHALITY
- TUMOR-SUPPRESSOR PROTEIN
- CELL-CYCLE ARREST
- IN-VIVO
- DNA-DAMAGE
- LIGASE ACTIVITY
- PROSTATE-CANCER
- MDM2 PROMOTES
- COLON-CANCER
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