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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| Format: | Article |
| Language: | English |
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MDPI AG
2021-05-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/10/5/1235 |
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| author | Meenakshi Basu-Shrivastava Alina Kozoriz Solange Desagher Iréna Lassot |
| author_facet | Meenakshi Basu-Shrivastava Alina Kozoriz Solange Desagher Iréna Lassot |
| author_sort | Meenakshi Basu-Shrivastava |
| collection | DOAJ |
| 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 <i>TRIM17</i> gene regulation and expression, TRIM17 protein structure and interactions, as well as its involvement in cell physiology and human disorders. |
| first_indexed | 2024-03-10T11:19:34Z |
| format | Article |
| id | doaj.art-f5ed34fb161b4503a1490733572dc366 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T11:19:34Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-f5ed34fb161b4503a1490733572dc3662023-11-21T20:11:05ZengMDPI AGCells2073-44092021-05-01105123510.3390/cells10051235To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and DeathMeenakshi Basu-Shrivastava0Alina Kozoriz1Solange Desagher2Iréna Lassot3Institut de Génétique Moléculaire de Montpellier, University Montpellier, CNRS, Montpellier, FranceInstitut de Génétique Moléculaire de Montpellier, University Montpellier, CNRS, Montpellier, FranceInstitut de Génétique Moléculaire de Montpellier, University Montpellier, CNRS, Montpellier, FranceInstitut de Génétique Moléculaire de Montpellier, University Montpellier, CNRS, Montpellier, FranceTRIM17 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 <i>TRIM17</i> gene regulation and expression, TRIM17 protein structure and interactions, as well as its involvement in cell physiology and human disorders.https://www.mdpi.com/2073-4409/10/5/1235TRIM17ubiquitinationproteolysisapoptosisautophagymitosis |
| spellingShingle | Meenakshi Basu-Shrivastava Alina Kozoriz Solange Desagher Iréna Lassot To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death Cells TRIM17 ubiquitination proteolysis apoptosis autophagy mitosis |
| 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 | TRIM17 ubiquitination proteolysis apoptosis autophagy mitosis |
| url | https://www.mdpi.com/2073-4409/10/5/1235 |
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