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Essential Roles of E3 Ubiquitin Ligases in p53 Regulation

The ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels and activities of p53 in a large range of phy...

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Autores principales: Sane, Sanam, Rezvani, Khosrow
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343976/
https://www.ncbi.nlm.nih.gov/pubmed/28218667
http://dx.doi.org/10.3390/ijms18020442
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author Sane, Sanam
Rezvani, Khosrow
author_facet Sane, Sanam
Rezvani, Khosrow
author_sort Sane, Sanam
collection PubMed
description The ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels and activities of p53 in a large range of physiological conditions and in response to cellular changes induced by exogenous and endogenous stresses. The regulation of p53’s functions by E3 ubiquitin ligases is a complex process that can lead to positive or negative regulation of p53 protein in a context- and cell type-dependent manner. Accessory proteins bind and modulate E3 ubiquitin ligases, adding yet another layer of regulatory control for p53 and its downstream functions. This review provides a comprehensive understanding of p53 regulation by selective E3 ubiquitin ligases and their potential to be considered as a new class of biomarkers and therapeutic targets in diverse types of cancers.
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spelling pubmed-53439762017-03-16 Essential Roles of E3 Ubiquitin Ligases in p53 Regulation Sane, Sanam Rezvani, Khosrow Int J Mol Sci Review The ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels and activities of p53 in a large range of physiological conditions and in response to cellular changes induced by exogenous and endogenous stresses. The regulation of p53’s functions by E3 ubiquitin ligases is a complex process that can lead to positive or negative regulation of p53 protein in a context- and cell type-dependent manner. Accessory proteins bind and modulate E3 ubiquitin ligases, adding yet another layer of regulatory control for p53 and its downstream functions. This review provides a comprehensive understanding of p53 regulation by selective E3 ubiquitin ligases and their potential to be considered as a new class of biomarkers and therapeutic targets in diverse types of cancers. MDPI 2017-02-17 /pmc/articles/PMC5343976/ /pubmed/28218667 http://dx.doi.org/10.3390/ijms18020442 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Sane, Sanam
Rezvani, Khosrow
Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title_full Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title_fullStr Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title_full_unstemmed Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title_short Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
title_sort essential roles of e3 ubiquitin ligases in p53 regulation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5343976/
https://www.ncbi.nlm.nih.gov/pubmed/28218667
http://dx.doi.org/10.3390/ijms18020442
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