The plot thickens: OTULIN regulation in cell death
We recently demonstrated that post-translational modifications of the OTU deubiquitinase with linear linkage specificity (OTULIN) regulate its function in cell death. OTULIN hyper-phosphorylation promotes necroptosis by locking ring finger protein 31 (RNF31, also known as HOIP) away from the cylindr...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2020-07-01
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| Series: | Molecular & Cellular Oncology |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/23723556.2020.1740541 |
| _version_ | 1797677156819533824 |
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| author | Todd Douglas Maya Saleh |
| author_facet | Todd Douglas Maya Saleh |
| author_sort | Todd Douglas |
| collection | DOAJ |
| description | We recently demonstrated that post-translational modifications of the OTU deubiquitinase with linear linkage specificity (OTULIN) regulate its function in cell death. OTULIN hyper-phosphorylation promotes necroptosis by locking ring finger protein 31 (RNF31, also known as HOIP) away from the cylindromatosis (CYLD) complex, resulting in altered receptor interacting serine/threonine kinase 1 (RIPK1) ubiquitination. Further, we identified dual specificity phosphatase 14 (DUSP14) as an OTULIN phosphatase that limits necroptosis. |
| first_indexed | 2024-03-11T22:40:57Z |
| format | Article |
| id | doaj.art-956a25a5266d435faa24a7e47ace4063 |
| institution | Directory Open Access Journal |
| issn | 2372-3556 |
| language | English |
| last_indexed | 2024-03-11T22:40:57Z |
| publishDate | 2020-07-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Molecular & Cellular Oncology |
| spelling | doaj.art-956a25a5266d435faa24a7e47ace40632023-09-22T09:11:01ZengTaylor & Francis GroupMolecular & Cellular Oncology2372-35562020-07-017410.1080/23723556.2020.17405411740541The plot thickens: OTULIN regulation in cell deathTodd Douglas0Maya Saleh1McGill UniversityMcGill UniversityWe recently demonstrated that post-translational modifications of the OTU deubiquitinase with linear linkage specificity (OTULIN) regulate its function in cell death. OTULIN hyper-phosphorylation promotes necroptosis by locking ring finger protein 31 (RNF31, also known as HOIP) away from the cylindromatosis (CYLD) complex, resulting in altered receptor interacting serine/threonine kinase 1 (RIPK1) ubiquitination. Further, we identified dual specificity phosphatase 14 (DUSP14) as an OTULIN phosphatase that limits necroptosis.http://dx.doi.org/10.1080/23723556.2020.1740541cell deathapoptosisnecroptosisotulinlubacripk1cylddusp14phosphorylationubiquitination |
| spellingShingle | Todd Douglas Maya Saleh The plot thickens: OTULIN regulation in cell death Molecular & Cellular Oncology cell death apoptosis necroptosis otulin lubac ripk1 cyld dusp14 phosphorylation ubiquitination |
| title | The plot thickens: OTULIN regulation in cell death |
| title_full | The plot thickens: OTULIN regulation in cell death |
| title_fullStr | The plot thickens: OTULIN regulation in cell death |
| title_full_unstemmed | The plot thickens: OTULIN regulation in cell death |
| title_short | The plot thickens: OTULIN regulation in cell death |
| title_sort | plot thickens otulin regulation in cell death |
| topic | cell death apoptosis necroptosis otulin lubac ripk1 cyld dusp14 phosphorylation ubiquitination |
| url | http://dx.doi.org/10.1080/23723556.2020.1740541 |
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