TRIM21 Regulates Virus-Induced Cell Pyroptosis through Polyubiquitination of ISG12a
Pyroptosis is a form of regulated cell death mediated by the gasdermin protein family. During virus infection, cell pyroptosis restricts viral replication. The mechanisms of the tripartite motif (TRIM) protein family and IFN-stimulated genes (ISGs) against viruses have been studied. The role of TRIM...
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| Veröffentlicht in: | The Journal of immunology (1950) 2022-11, Vol.209 (10), p.1987-1998 |
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| container_end_page | 1998 |
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| container_issue | 10 |
| container_start_page | 1987 |
| container_title | The Journal of immunology (1950) |
| container_volume | 209 |
| creator | Guo, Mengmeng Cao, Wenyan Chen, Shengwen Tian, Renyun Xue, Binbin Wang, Luoling Liu, Qian Deng, Rilin Wang, Xintao Wang, Zhenghao Zhang, Yingdan Yang, Di Zuo, Chaohui Li, Guangdi Tang, Songqing Zhu, Haizhen |
| description | Pyroptosis is a form of regulated cell death mediated by the gasdermin protein family. During virus infection, cell pyroptosis restricts viral replication. The mechanisms of the tripartite motif (TRIM) protein family and IFN-stimulated genes (ISGs) against viruses have been studied. The role of TRIMs and ISGs in pyroptosis remains unclear. In this study, we show that TRIM21 interacts with ISG12a in viral infection and facilitates its translocation into the mitochondria by promoting its ubiquitination, thereby causing caspase 3 activation. Gasdermin E (GSDME) is specifically cleaved by caspase 3 upon viral infection, releasing the GSDME N-terminal domain, perforating the cell membrane, and causing cell pyroptosis. Our study uncovers a new mechanism of TRIM21 and ISG12a in regulating virus-induced cell pyroptosis. |
| doi_str_mv | 10.4049/jimmunol.2200163 |
| format | Article |
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During virus infection, cell pyroptosis restricts viral replication. The mechanisms of the tripartite motif (TRIM) protein family and IFN-stimulated genes (ISGs) against viruses have been studied. The role of TRIMs and ISGs in pyroptosis remains unclear. In this study, we show that TRIM21 interacts with ISG12a in viral infection and facilitates its translocation into the mitochondria by promoting its ubiquitination, thereby causing caspase 3 activation. Gasdermin E (GSDME) is specifically cleaved by caspase 3 upon viral infection, releasing the GSDME N-terminal domain, perforating the cell membrane, and causing cell pyroptosis. 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During virus infection, cell pyroptosis restricts viral replication. The mechanisms of the tripartite motif (TRIM) protein family and IFN-stimulated genes (ISGs) against viruses have been studied. The role of TRIMs and ISGs in pyroptosis remains unclear. In this study, we show that TRIM21 interacts with ISG12a in viral infection and facilitates its translocation into the mitochondria by promoting its ubiquitination, thereby causing caspase 3 activation. Gasdermin E (GSDME) is specifically cleaved by caspase 3 upon viral infection, releasing the GSDME N-terminal domain, perforating the cell membrane, and causing cell pyroptosis. 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Caspase 3 - metabolism Cell Death Pyroptosis - physiology Tripartite Motif Proteins - metabolism Ubiquitination Viruses |
| title | TRIM21 Regulates Virus-Induced Cell Pyroptosis through Polyubiquitination of ISG12a |
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