Evidence map›Paper›PMID 41271597›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Tissue-Resident Macrophage-Derived E3 Ligase SMURF2 Restricts Autoimmune Inflammation by Mediating the Degradation of p-TBK1.

Xiang An, Jun Li, Lingling Wang, Chengyuan Li, Zhenpeng Jin, Yushi Yao, Minmin Jiang, Wenlong Lin, Xiaojian Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Xiang AnInstitute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310058, China.
Jun LiDepartment of Pathology, the First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310003, China.
Lingling WangInstitute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310058, China.
Chengyuan LiInstitute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310058, China.
Zhenpeng JinInstitute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310058, China.
Yushi YaoLiangzhu Laboratory, Zhejiang University Medical Center, 1369 West Wenyi Road, Hangzhou, 311121, China.
Minmin JiangShulan International Medical College, Zhejiang Shuren University, Hangzhou, 310015, China.
Wenlong LinThe Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Xiaojian WangInstitute of Immunology and Bone Marrow Transplantation Center of The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, 310058, China.ORCID https://orcid.org/0000-0001-8232-0558

Funding

China Postdoctoral Science Foundation 2024M762909National Natural Science Foundation of China 82171735National Natural Science Foundation of China 82371763
6 · The paper itself

Abstract

Dysregulated tissue-resident macrophages (TRMs) contribute to the pathogenesis of inflammatory bowel disease (IBD) and multiple sclerosis (MS). Uncovering molecular regulators of the divergent role of TRMs in inflammation can advance therapeutic strategies for autoimmune disorders. Here, a significant downregulation of SMAD-specific E3 ubiquitin protein ligase 2 (SMURF2) is reported in TRMs within inflamed intestinal tissues from both IBD patients and mouse models. Notably, TRM-specific deficiency of Smurf2 significantly exacerbates TRM proliferation in dextran sulfate sodium (DSS)-induced colitis and experimental autoimmune encephalomyelitis (EAE), leading to augmented autoimmune inflammation. Mechanistically, SMURF2 interacts with phosphorylated TBK1 (p-TBK1), mediating its Lys-27-linked 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-TBK1 modulation. Given that impaired SMURF2 expression correlates with the progression of autoimmune inflammation, SMURF2 represents a potential target for autoimmune disease treatment.

Indexed as

Encephalomyelitis, Autoimmune, ExperimentalInflammationMacrophagesProtein Serine-Threonine KinasesUbiquitin-Protein LigasesAnimalsColitisDisease Models, AnimalFemaleHumansInflammatory Bowel DiseasesMiceMice, Inbred C57BLPhosphorylationUbiquitinationProtein Serine-Threonine KinasesSMURF2 protein, humanSmurf2 protein, mouseTBK1 protein, humanTbk1 protein, mouseUbiquitin-Protein Ligasesautoimmune diseasesinflammatory bowel diseasep‐TBK1tissue‐resident macrophagesubiquitination

Identifiers

PMID41271597
PMCPMC12866865

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.