{"title":"通过相分离调节RIG-I活性揭示了新的治疗机会","authors":"","doi":"10.1038/s41556-025-01656-3","DOIUrl":null,"url":null,"abstract":"After virus infection, RIG-I forms disulfide-linked oligomers that are resistant to degradation and able to enter liquid-like condensates, which is necessary for RIG-I-mediated stimulation of type I interferon signalling. RIG-I agonists and antagonists that enhance or prevent formation of disulfide-linked RIG-I oligomers, respectively, confirm that this mechanism is crucial for RIG-I function and could be harnessed to boost antiviral immunity or suppress autoimmunity caused by hyperactive RIG-I.","PeriodicalId":18977,"journal":{"name":"Nature Cell Biology","volume":"2 1","pages":""},"PeriodicalIF":17.3000,"publicationDate":"2025-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Regulation of RIG-I activity by phase separation reveals new therapeutic opportunities\",\"authors\":\"\",\"doi\":\"10.1038/s41556-025-01656-3\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"After virus infection, RIG-I forms disulfide-linked oligomers that are resistant to degradation and able to enter liquid-like condensates, which is necessary for RIG-I-mediated stimulation of type I interferon signalling. RIG-I agonists and antagonists that enhance or prevent formation of disulfide-linked RIG-I oligomers, respectively, confirm that this mechanism is crucial for RIG-I function and could be harnessed to boost antiviral immunity or suppress autoimmunity caused by hyperactive RIG-I.\",\"PeriodicalId\":18977,\"journal\":{\"name\":\"Nature Cell Biology\",\"volume\":\"2 1\",\"pages\":\"\"},\"PeriodicalIF\":17.3000,\"publicationDate\":\"2025-05-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Cell Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1038/s41556-025-01656-3\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Cell Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1038/s41556-025-01656-3","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
Regulation of RIG-I activity by phase separation reveals new therapeutic opportunities
After virus infection, RIG-I forms disulfide-linked oligomers that are resistant to degradation and able to enter liquid-like condensates, which is necessary for RIG-I-mediated stimulation of type I interferon signalling. RIG-I agonists and antagonists that enhance or prevent formation of disulfide-linked RIG-I oligomers, respectively, confirm that this mechanism is crucial for RIG-I function and could be harnessed to boost antiviral immunity or suppress autoimmunity caused by hyperactive RIG-I.
期刊介绍:
Nature Cell Biology, a prestigious journal, upholds a commitment to publishing papers of the highest quality across all areas of cell biology, with a particular focus on elucidating mechanisms underlying fundamental cell biological processes. The journal's broad scope encompasses various areas of interest, including but not limited to:
-Autophagy
-Cancer biology
-Cell adhesion and migration
-Cell cycle and growth
-Cell death
-Chromatin and epigenetics
-Cytoskeletal dynamics
-Developmental biology
-DNA replication and repair
-Mechanisms of human disease
-Mechanobiology
-Membrane traffic and dynamics
-Metabolism
-Nuclear organization and dynamics
-Organelle biology
-Proteolysis and quality control
-RNA biology
-Signal transduction
-Stem cell biology