Evidence map›Paper›PMID 42702386›Full record

ReviewZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences2026

[Ubiquitination-mediated regulation of T cell homeostasis and autoimmune diseases].

Mengdi Zhang, Mingjiu Zhao, Jiaqi Huang, Zhiguang Zhou, Bin Zhao

Abstract readReviewEnglish Abstract
In one paragraph

Review in Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Mengdi ZhangNational Clinical Research Center for Endocrine and Metabolic Diseases, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, Second Xiangya Hospital, Central South University, Changsha 410011. zmd199301@163.com.
Mingjiu ZhaoNational Clinical Research Center for Endocrine and Metabolic Diseases, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, Second Xiangya Hospital, Central South University, Changsha 410011.
Jiaqi HuangNational Clinical Research Center for Endocrine and Metabolic Diseases, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, Second Xiangya Hospital, Central South University, Changsha 410011.
Zhiguang ZhouNational Clinical Research Center for Endocrine and Metabolic Diseases, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, Second Xiangya Hospital, Central South University, Changsha 410011.
Bin ZhaoNational Clinical Research Center for Endocrine and Metabolic Diseases, Key Laboratory of Diabetes Immunology, Ministry of Education, and Department of Metabolism and Endocrinology, Second Xiangya Hospital, Central South University, Changsha 410011. binzhao@csu.edu.cn.

Funding

the Scientific Research Program of Furong Laboratory (the Program of the Department of Science and Technology of Hunan Province) 2024PT5105
6 · The paper itself

Abstract

Ubiquitination is a highly dynamic and reversible post-translational modification that is extensively involved in protein degradation, signal transduction, and functional regulation in eukaryotic cells. Through the coordinated action of the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin-protein ligase (E3) cascade, ubiquitin molecules are conjugated to substrate proteins through distinct ubiquitin chain linkages, thereby determining proteasomal degradation, subcellular trafficking, or non-degradative scaffold functions of target proteins. In the immune system, E3 ligases and deubiquitinases (DUBs) precisely regulate T cell antigen recognition, receptor signaling, activation, proliferation, and effector differentiation by controlling substrate selection and ubiquitin chain editing. By modulating the stability of T cell receptors, co-stimulatory and cytokine signaling molecules, as well as key transcription factors and metabolic regulators, E3 ligases and DUBs influence T cell activation thresholds, anergic states, survival, and differentiation programs. Together, they constitute an essential regulatory network responsible for maintaining T cell homeostasis and peripheral immune tolerance. Dysregulation of this network can enhance pro-inflammatory T cell responses and impaired regulatory T cell function, thereby weakening peripheral immune tolerance and contributing to the development and progression of various autoimmune diseases, including systemic lupus erythematosus, rheumatoid arthritis, and type 1 diabetes mellitus. Systematic summarization of the molecular mechanisms and key signaling pathways through which E3 ligases and DUBs regulate T cell fate, together with elucidation of substrate landscapes, ubiquitin chain preferences, and their metabolic crosstalk among different T cell subsets, will deepen our understanding of how ubiquitination maintains T cell homeostasis and contributes to autoimmune disease pathogenesis. Furthermore, such insights may provide a theoretical foundation and translational directions for the development of chain-specific and cell-type-selective therapeutic strategies.

Indexed as

Autoimmune DiseasesHomeostasisT-LymphocytesUbiquitinationAnimalsHumansSignal TransductionUbiquitin-Protein LigasesUbiquitin-Protein Ligasesautoimmune diseasesdeubiquitinationT cell differentiationT cell homeostasisubiquitination

Identifiers

PMID42702386
PMCPMC13500737

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.