Evidence map›Paper›PMID 36337049›Full record

ArticleCirculation research2022

Blocking MG53

Fengxiang Lv, Yingfan Wang, Dan Shan, Sile Guo, Gengjia Chen, Li Jin, Wen Zheng, Han Feng, Xiaohu Zeng, Shuo Zhang and 3 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Circulation research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
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

17 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  14. Review
  15. E3 ligase MG53 suppresses tumor growth by degrading cyclin D1.Signal transduction and targeted therapy · 2023
    Article
  16. Is MG53 a potential therapeutic target for cancer?Frontiers in endocrinology · 2023
    Review
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

Fengxiang Lv *State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).ORCID 0000-0002-9535-1326
Yingfan Wang *State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Dan Shan *State Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Sile GuoState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).ORCID 0000-0002-8070-2760
Gengjia ChenState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Li JinState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Wen ZhengState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Han FengState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Xiaohu ZengState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Shuo ZhangState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).
Yan ZhangState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).ORCID 0000-0002-8322-467X
Xinli HuState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).ORCID 0000-0003-4911-5354
Rui-Ping XiaoState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, College of Future Technology, Peking University, Beijing, China (F.L., Y.W., D.S., S.G., G.C., L.J., W.Z., H.F., X.Z., S.Z., Y.Z., X.H., R.-P.X.).ORCID 0000-0003-2448-409X
Xerox (France) · FRKing University · USPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAs an integral component of cell membrane repair machinery, MG53 (mitsugumin 53) is important for cardioprotection induced by ischemia preconditioning and postconditioning. However, it also impairs insulin signaling via its E3 ligase activity-mediated ubiquitination-dependent degradation of IR (insulin receptor) and IRS1 (insulin receptor substrate 1) and its myokine function-induced allosteric blockage of IR. Here, we sought to develop MG53 into a cardioprotection therapy by separating its detrimental metabolic effects from beneficial actions.

methodsUsing immunoprecipitation-mass spectrometry, site-specific mutation, in vitro kinase assay, and in vivo animal studies, we investigated the role of MG53 phosphorylation at serine 255 (S255). In particular, utilizing recombinant proteins and gene knock-in approaches, we evaluated the potential therapeutic effect of MG53-S255A mutant in treating cardiac ischemia/reperfusion injury in diabetic mice.

resultsWe identified S255 phosphorylation as a prerequisite for MG53 E3 ligase activity. Furthermore, MG53

conclusionsS255 phosphorylation is a biased regulation of MG53 E3 ligase activity. The MG53-S255A mutant provides a promising approach for the treatment of acute myocardial injury, especially in patients with metabolic disorders.

Indexed as

Diabetes Mellitus, ExperimentalReperfusion InjuryAnimalsCarrier ProteinsGlycogen Synthase Kinase 3 betaInsulinIschemiaMembrane ProteinsMicePhosphorylationSerineUbiquitin-Protein LigasesCarrier ProteinsGlycogen Synthase Kinase 3 betaInsulinMembrane ProteinsMG53 protein, mouseSerineUbiquitin-Protein Ligasescardiac ischemia/reperfusion injurycardioprotectionGSK3βinsulin resistanceMG53

Identifiers

PMID36337049
PMCPMC9770150
OpenAlexW4308371478

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.