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To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death

TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the tr...

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Autores principales: Basu-Shrivastava, Meenakshi, Kozoriz, Alina, Desagher, Solange, Lassot, Iréna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157266/
https://www.ncbi.nlm.nih.gov/pubmed/34069831
http://dx.doi.org/10.3390/cells10051235
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author Basu-Shrivastava, Meenakshi
Kozoriz, Alina
Desagher, Solange
Lassot, Iréna
author_facet Basu-Shrivastava, Meenakshi
Kozoriz, Alina
Desagher, Solange
Lassot, Iréna
author_sort Basu-Shrivastava, Meenakshi
collection PubMed
description TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses. As most TRIM members, TRIM17 can act as an E3 ubiquitin-ligase and promote the degradation by the proteasome of substrates such as the antiapoptotic protein MCL1. Intriguingly, TRIM17 can also prevent the ubiquitination of other proteins and stabilize them, by binding to other TRIM proteins and inhibiting their E3 ubiquitin-ligase activity. This duality of action confers several pivotal roles to TRIM17 in crucial cellular processes such as apoptosis, autophagy or cell division, but also in pathological conditions as diverse as Parkinson’s disease or cancer. Here, in addition to recent data that endorse this duality, we review what is currently known from public databases and the literature about TRIM17 gene regulation and expression, TRIM17 protein structure and interactions, as well as its involvement in cell physiology and human disorders.
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spelling pubmed-81572662021-05-28 To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death Basu-Shrivastava, Meenakshi Kozoriz, Alina Desagher, Solange Lassot, Iréna Cells Review TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses. As most TRIM members, TRIM17 can act as an E3 ubiquitin-ligase and promote the degradation by the proteasome of substrates such as the antiapoptotic protein MCL1. Intriguingly, TRIM17 can also prevent the ubiquitination of other proteins and stabilize them, by binding to other TRIM proteins and inhibiting their E3 ubiquitin-ligase activity. This duality of action confers several pivotal roles to TRIM17 in crucial cellular processes such as apoptosis, autophagy or cell division, but also in pathological conditions as diverse as Parkinson’s disease or cancer. Here, in addition to recent data that endorse this duality, we review what is currently known from public databases and the literature about TRIM17 gene regulation and expression, TRIM17 protein structure and interactions, as well as its involvement in cell physiology and human disorders. MDPI 2021-05-18 /pmc/articles/PMC8157266/ /pubmed/34069831 http://dx.doi.org/10.3390/cells10051235 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Basu-Shrivastava, Meenakshi
Kozoriz, Alina
Desagher, Solange
Lassot, Iréna
To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title_full To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title_fullStr To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title_full_unstemmed To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title_short To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
title_sort to ubiquitinate or not to ubiquitinate: trim17 in cell life and death
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8157266/
https://www.ncbi.nlm.nih.gov/pubmed/34069831
http://dx.doi.org/10.3390/cells10051235
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