ORIGINAL RESEARCH article
Front. Immunol.
Sec. Inflammation
Volume 16 - 2025 | doi: 10.3389/fimmu.2025.1593243
This article is part of the Research TopicRegulation of Inflammation: Metabolic Reprogramming and Posttranslational ModificationView all articles
FTO O-GlcNAcylation promotes TRIM21-mediated FTO ubiquitination degradation to sustain the negative feedback control of macrophage inflammation
Provisionally accepted
- 1Hubei Province Key Laboratory of Allergy and Immunology, and Department of Immunology Wuhan University School of Basic Medical Sciences, Wuhan 430071, China, Wuhan, Hebei Province, China
- 2Department of Immunology, School of Basic Medical Sciences, Wuhan University, Wuhan, Hubei Province, China
- 3Wuhan University, Wuhan, China
- 4Allergy Department of Zhongnan Hospital, State Key Laboratory of Virology, Medical Research Institute Wuhan University School of Medicine, Wuhan 430071, China, Wuhan, Hebei Province, China
- 5School of Public Health, Faculty of Medical Sciences, Wuhan University, Wuhan, Hubei Province, China
- 6Department of Critical Care Medicine, Zhongnan Hospital, Wuhan University, Wuhan, Hubei Province, China
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The fat mass and obesity-associated protein (FTO), a key RNA N 6methyladenosine (m 6 A) demethylase, has been highlighted for its important role in inflammatory response. Emerging evidences link the O-GlcNAcylation to numerous human diseases, particularly inflammation. However, the specific role and underlying mechanism of FTO O-GlcNAcylation in inflammation remain elusive.The FTO O-GlcNAcylation modification was determined by coimmunoprecipitation (Co-IP) assay, metabolic glycan labeling combined with click reaction, and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis.Chromatin immunoprecipitation (ChIP)-qPCR and dual-luciferase reporter assay were used to determine FOXO1 binding to the Gfat2 promoter and the Gfat2 promoter activity during LPS stimulation. The FTO ubiquitination modification and the interaction between FTO and TRIM21 were detected by confocal microscopy, pull-down, and mass
Keywords: FTO, O-GlcNAcylation, Ubiquitination, macrophage, Inflammatory Response
Received: 13 Mar 2025; Accepted: 10 Jun 2025.
Copyright: © 2025 Zhang, Zhang, Liu, Xie, Yuan, Peng and Xiong. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Xiao-Lian Zhang, Wuhan University, Wuhan, China
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