Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy

Nerea Allende-Vega; Mark K. Saville

doi:10.1016/j.semcancer.2009.10.004

Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy

Nerea Allende-Vega, Mark K. Saville

Research output: Contribution to journal › Review article › peer-review

41 Citations (Scopus)

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	https://doi.org/10.1016/j.semcancer.2009.10.004
Publication status	Published - Feb 2010

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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.semcancer.2009.10.004

Cite this

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title = "Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy",

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.",

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author = "Nerea Allende-Vega and Saville, {Mark K.}",

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AU - Allende-Vega, Nerea

AU - Saville, Mark K.

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AB - 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.

KW - Ubiquitin

KW - P53

KW - Mdm2

KW - MdmX

KW - 26S proteasome

KW - E1

KW - E2

KW - E3

KW - Deubiquitinating enzyme

KW - SMALL-MOLECULE INHIBITORS

KW - EARLY EMBRYONIC LETHALITY

KW - TUMOR-SUPPRESSOR PROTEIN

KW - CELL-CYCLE ARREST

KW - IN-VIVO

KW - DNA-DAMAGE

KW - LIGASE ACTIVITY

KW - PROSTATE-CANCER

KW - MDM2 PROMOTES

KW - COLON-CANCER

U2 - 10.1016/j.semcancer.2009.10.004

DO - 10.1016/j.semcancer.2009.10.004

M3 - Review article

C2 - 19897040

SN - 1044-579X

VL - 20

SP - 29

EP - 39

JO - Seminars in Cancer Biology

JF - Seminars in Cancer Biology

IS - 1

ER -

Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy

Abstract

Keywords

UN SDGs

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