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Uncovering molecular regulators of the divergent role of TRMs in inflammation can advance therapeutic strategies for autoimmune disorders. Here, a significant downregulation of SMAD\u2010specific E3 ubiquitin protein ligase 2 (SMURF2) is reported in TRMs within inflamed intestinal tissues from both IBD patients and mouse models. Notably, TRM\u2010specific deficiency of\n                    <jats:italic>Smurf2<\/jats:italic>\n                    significantly exacerbates TRM proliferation in dextran sulfate sodium (DSS)\u2010induced colitis and experimental autoimmune encephalomyelitis (EAE), leading to augmented autoimmune inflammation. Mechanistically, SMURF2 interacts with phosphorylated TBK1 (p\u2010TBK1), mediating its Lys\u201027\u2010linked ubiquitination and its subsequent lysosomal degradation, thereby suppressing TRM proliferation and autoimmune inflammation. Collectively, these findings establish SMURF2 as a pivotal mediator of TRM proliferation and autoimmune inflammation via p\u2010TBK1 modulation. Given that impaired SMURF2 expression correlates with the progression of autoimmune inflammation, SMURF2 represents a potential target for autoimmune disease treatment.\n                  <\/jats:p>","DOI":"10.1002\/advs.202504930","type":"journal-article","created":{"date-parts":[[2025,11,22]],"date-time":"2025-11-22T03:46:03Z","timestamp":1763783163000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Tissue\u2010Resident Macrophage\u2010Derived E3 Ligase SMURF2 Restricts Autoimmune Inflammation by Mediating the Degradation of p\u2010TBK1"],"prefix":"10.1002","volume":"13","author":[{"given":"Xiang","family":"An","sequence":"first","affiliation":[{"name":"Institute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital School of Medicine Zhejiang University  Hangzhou 310058 China"},{"name":"Liangzhu Laboratory Zhejiang University Medical Center  1369 West Wenyi Road Hangzhou 311121 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