Evidence map›Paper›PMID 39847321›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

The LIM-domain-only protein LMO2 and its binding partner LDB1 are differentially required for class switch recombination.

Beibei Yang, Yao Guo, Lilong Liu, Ting Huang, Bo Zhao, Wanyu Bai, Guigen Zhang, Chengming Zhu, Junchao Dong

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. 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. Article
  2. The LIM-domain-only protein LMO2 and its binding partner LDB1 are differentially required for class switch recombination.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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.

Beibei Yang *Scientific Research Center, The Seventh Affiliated Hospital, Sun Yat-Sen University, Shenzhen, Guangdong 518107, China.ORCID 0009-0002-9589-6358
Yao Guo *Department of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.
Lilong LiuDepartment of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.
Ting HuangDepartment of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.
Bo ZhaoDepartment of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.
Wanyu BaiDepartment of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.
Guigen ZhangInstitute of Human Virology, Department of Pathogen Biology and Biosecurity, and Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.ORCID 0000-0002-3336-6768
Chengming ZhuScientific Research Center, The Seventh Affiliated Hospital, Sun Yat-Sen University, Shenzhen, Guangdong 518107, China.
Junchao DongDepartment of Immunology and Microbiology, Key Laboratory of Tropical Disease Control of Ministry of Education, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, Guangdong 510000, China.

Funding

MOST | National Natural Science Foundation of China (NSFC) 81871304 32070892 32270934Open Fund of Guangdong Provincial Key Laboratory of Digestive Cancer Research 2021B1212040006| Sanming Project of Medicine in Shenzen Municipality (Sanming Project of Medicine in Shenzhen) SZSM202011004
6 · The paper itself

Abstract

The LIM-domain-only protein LMO2 interacts with LDB1 in context-dependent multiprotein complexes and plays key roles in erythropoiesis and T cell leukemogenesis, but whether they have any roles in B cells is unclear. Through a CRISPR/Cas9-based loss-of-function screening, we identified LMO2 and LDB1 as factors for class switch recombination (CSR) in murine B cells. LMO2 contributes to CSR at least in part by promoting end joining of DNA double-strand breaks (DSBs) and inhibiting end resection. Although LDB1 stabilizes LMO2 proteins, it is not required for end joining but functions as a positive regulator of AID transcription independent of LMO2, and this function of LDB1 requires its dimerization domain. Moreover, LDB1 directly binds to and promotes the looping of the AID promoter to upstream enhancers through dimerization. Our study revealed the mechanistically separated roles of LMO2 and LDB1 in different steps of CSR for antibody diversification.

Indexed as

Adaptor Proteins, Signal TransducingDNA-Binding ProteinsImmunoglobulin Class SwitchingLIM Domain ProteinsAnimalsB-LymphocytesDioxygenasesDNA Breaks, Double-StrandedHumansMiceProtein BindingAdaptor Proteins, Signal TransducingDioxygenasesDNA-Binding ProteinsLdb1 protein, mouseLIM Domain ProteinsLmo2 protein, mouseB cellsclass switch recombinationDSB resectionLMO2/LDB1promoter–enhancer looping

Identifiers

PMID39847321
PMCPMC11789033

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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.