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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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. |
format | Online Article Text |
id | pubmed-8157266 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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