HECT E3 Ligases: A Tale With Multiple Facets

Ubiquitination plays a pivotal role in several cellular processes and is critical for protein degradation and signaling. E3 ubiquitin ligases are the matchmakers in the ubiquitination cascade, responsible for substrate recognition. In order to achieve selectivity and specificity on their substrates,...

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Detalles Bibliográficos
Autores principales: Weber, Janine, Polo, Simona, Maspero, Elena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Physiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6457168/
https://www.ncbi.nlm.nih.gov/pubmed/31001145
http://dx.doi.org/10.3389/fphys.2019.00370
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author Weber, Janine
Polo, Simona
Maspero, Elena
author_facet Weber, Janine
Polo, Simona
Maspero, Elena
author_sort Weber, Janine
collection PubMed
description Ubiquitination plays a pivotal role in several cellular processes and is critical for protein degradation and signaling. E3 ubiquitin ligases are the matchmakers in the ubiquitination cascade, responsible for substrate recognition. In order to achieve selectivity and specificity on their substrates, HECT E3 enzymes are tightly regulated and exert their function in a spatially and temporally controlled fashion in the cells. These characteristics made HECT E3s intriguing targets in drug discovery in the context of cancer biology.
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spelling pubmed-64571682019-04-18 HECT E3 Ligases: A Tale With Multiple Facets Weber, Janine Polo, Simona Maspero, Elena Front Physiol Physiology Ubiquitination plays a pivotal role in several cellular processes and is critical for protein degradation and signaling. E3 ubiquitin ligases are the matchmakers in the ubiquitination cascade, responsible for substrate recognition. In order to achieve selectivity and specificity on their substrates, HECT E3 enzymes are tightly regulated and exert their function in a spatially and temporally controlled fashion in the cells. These characteristics made HECT E3s intriguing targets in drug discovery in the context of cancer biology. Frontiers Media S.A. 2019-04-03 /pmc/articles/PMC6457168/ /pubmed/31001145 http://dx.doi.org/10.3389/fphys.2019.00370 Text en Copyright © 2019 Weber, Polo and Maspero. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Weber, Janine
Polo, Simona
Maspero, Elena
HECT E3 Ligases: A Tale With Multiple Facets
title HECT E3 Ligases: A Tale With Multiple Facets
title_full HECT E3 Ligases: A Tale With Multiple Facets
title_fullStr HECT E3 Ligases: A Tale With Multiple Facets
title_full_unstemmed HECT E3 Ligases: A Tale With Multiple Facets
title_short HECT E3 Ligases: A Tale With Multiple Facets
title_sort hect e3 ligases: a tale with multiple facets
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6457168/
https://www.ncbi.nlm.nih.gov/pubmed/31001145
http://dx.doi.org/10.3389/fphys.2019.00370
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AT polosimona hecte3ligasesatalewithmultiplefacets
AT masperoelena hecte3ligasesatalewithmultiplefacets

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