دورية أكاديمية
Priming of NLRP3 inflammasome activation by Msn kinase MINK1 in macrophages.
العنوان: | Priming of NLRP3 inflammasome activation by Msn kinase MINK1 in macrophages. |
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المؤلفون: | Zhu K; Institute of Immunology and Department of Rheumatology, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China.; Zhejiang University-University of Edinburgh Institute, Zhejiang University School of Medicine, Haining, 314400, P. R. China.; Department of Medical Microbiology and Parasitology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Jin X; Institute of Immunology and Department of Rheumatology, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Chi Z; Department of Immunology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Chen S; Department of Immunology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China.; Department of Colorectal Surgery, The Second Affiliated Hospital, Hangzhou, 310058, P. R. China., Wu S; Medical College, Lishui University, Lishui, 323000, P. R. China., Sloan RD; Zhejiang University-University of Edinburgh Institute, Zhejiang University School of Medicine, Haining, 314400, P. R. China.; Infection Medicine, School of Biomedical Sciences, The University of Edinburgh, Edinburgh, EH16 4SB, Scotland, UK., Lin X; Department of Medical Microbiology and Parasitology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Neculai D; Department of Cell Biology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Wang D; Department of Immunology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Hu H; Department of Pathology and Pathophysiology, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China., Lu L; Institute of Immunology and Department of Rheumatology, Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China. lu_linrong@zju.edu.cn.; Zhejiang University-University of Edinburgh Institute, Zhejiang University School of Medicine, Haining, 314400, P. R. China. lu_linrong@zju.edu.cn.; Dr. Li Dak Sum and Yip Yio Chin Center for Stem Cells and Regenerative Medicine, Zhejiang University School of Medicine, Hangzhou, 310058, P. R. China. lu_linrong@zju.edu.cn. |
المصدر: | Cellular & molecular immunology [Cell Mol Immunol] 2021 Oct; Vol. 18 (10), pp. 2372-2382. Date of Electronic Publication: 2021 Sep 03. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Chinese Society of Immunology;; _b Nature Pub. Group Country of Publication: China NLM ID: 101242872 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2042-0226 (Electronic) Linking ISSN: 16727681 NLM ISO Abbreviation: Cell Mol Immunol Subsets: MEDLINE |
أسماء مطبوعة: | Original Publication: Beijing, China : Tokyo, Japan : Chinese Society of Immunology; Nature Pub. Group, 2010- |
مواضيع طبية MeSH: | Inflammasomes* , NLR Family, Pyrin Domain-Containing 3 Protein*, Animals ; Inflammation ; Macrophages ; Mice ; Reactive Oxygen Species |
مستخلص: | The nucleotide-binding domain, leucine-rich-repeat containing family, pyrin domain-containing 3 (NLRP3) inflammasome is essential in inflammation and inflammatory disorders. Phosphorylation at various sites on NLRP3 differentially regulates inflammasome activation. The Ser725 phosphorylation site on NLRP3 is depicted in multiple inflammasome activation scenarios, but the importance and regulation of this site has not been clarified. The present study revealed that the phosphorylation of Ser725 was an essential step for the priming of the NLRP3 inflammasome in macrophages. We also showed that Ser725 was directly phosphorylated by misshapen (Msn)/NIK-related kinase 1 (MINK1), depending on the direct interaction between MINK1 and the NLRP3 LRR domain. MINK1 deficiency reduced NLRP3 activation and suppressed inflammatory responses in mouse models of acute sepsis and peritonitis. Reactive oxygen species (ROS) upregulated the kinase activity of MINK1 and subsequently promoted inflammasome priming via NLRP3 Ser725 phosphorylation. Eliminating ROS suppressed NLRP3 activation and reduced sepsis and peritonitis symptoms in a MINK1-dependent manner. Altogether, our study reveals a direct regulation of the NLRP3 inflammasome by Msn family kinase MINK1 and suggests that modulation of MINK1 activity is a potential intervention strategy for inflammasome-related diseases. (© 2021. The Author(s), under exclusive licence to CSI and USTC.) |
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فهرسة مساهمة: | Keywords: MINK1 kinase; NLRP3 inflammasome; Phosphorylation; ROS |
المشرفين على المادة: | 0 (Inflammasomes) 0 (NLR Family, Pyrin Domain-Containing 3 Protein) 0 (Nlrp3 protein, mouse) 0 (Reactive Oxygen Species) |
تواريخ الأحداث: | Date Created: 20210904 Date Completed: 20220331 Latest Revision: 20230205 |
رمز التحديث: | 20240628 |
مُعرف محوري في PubMed: | PMC8414466 |
DOI: | 10.1038/s41423-021-00761-1 |
PMID: | 34480147 |
قاعدة البيانات: | MEDLINE |
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