Evidence map›Paper›PMID 39715739›Full record

ArticleCell death & disease2024

CARM1-mediated OGT arginine methylation promotes non-small cell lung cancer glycolysis by stabilizing OGT.

Luyao Lin, Qingxia Yuan, Jiayi Gu, Guangyu Bai, Xianling Cong, Qianying Hu, Jingyao Hou, Xin Jin, Xiangxiang Liu, Baiqu Huang and 2 more

Abstract read
In one paragraph

Article in Cell death & disease, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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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

12 authors.

Luyao LinThe Key Laboratory of Molecular Epigenetics of Ministry of Education (MOE), Northeast Normal University, 130024, Changchun, China.
Qingxia YuanThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Jiayi GuThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Guangyu BaiThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Xianling CongDepartment of Biobank, China-Japan Union Hospital of Jilin University, 130033, Changchun, China.ORCID 0000-0002-5790-4188
Qianying HuDepartment of Biobank, China-Japan Union Hospital of Jilin University, 130033, Changchun, China.
Jingyao HouThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Xin JinThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Xiangxiang LiuThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Baiqu HuangThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China.
Yu ZhangThe Key Laboratory of Molecular Epigenetics of Ministry of Education (MOE), Northeast Normal University, 130024, Changchun, China.
Jun LuThe Institute of Genetics and Cytology, Northeast Normal University, 130024, Changchun, China. luj809@nenu.edu.cn.ORCID 0000-0002-9141-6786

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32071292National Natural Science Foundation of China (National Science Foundation of China) 32171163National Natural Science Foundation of China (National Science Foundation of China) 32271207National Natural Science Foundation of China (National Science Foundation of China) 32371216
6 · The paper itself

Abstract

O-GlcNAcylation catalyzed by O-GlcNAc transferase (OGT) plays an important role in the regulation of tumor glycolysis. However, the mechanism underlying OGT regulation remains largely unknown. Here, we showed that coactivator associated arginine methyltransferase 1 (CARM1) sensed changes of extracellular glucose levels in non-small cell lung cancer (NSCLC) cells. Increased glucose upregulated CARM1 and OGT. CARM1 methylated OGT at arginine 348, promoting its stability through binding of the deubiquitinase USP9X. The arginine methylation of OGT increased global O-GlcNAcylation levels, thereby promoting glycolysis in NSCLC cells. OGT arginine methylation also upregulated c-Myc expression and promoted the proliferation of NSCLC cells in vitro and in vivo. Consistently, OGT expression was positively correlated with CARM1 in human NSCLC samples. The present findings shed light on the mechanism underlying the stabilization of OGT by arginine methylation in response to changes of glucose concentration. The study also clarified the role of the CARM1-USP9X-OGT axis in glycolysis in NSCLC, providing a potential new target or therapeutic strategy in NSCLC.

Indexed as

ArginineCarcinoma, Non-Small-Cell LungGlycolysisLung NeoplasmsN-AcetylglucosaminyltransferasesProtein-Arginine N-MethyltransferasesAnimalsCell Line, TumorCell ProliferationFemaleGene Expression Regulation, NeoplasticGlucoseHumansMaleMethylationMiceArgininecoactivator-associated arginine methyltransferase 1GlucoseN-AcetylglucosaminyltransferasesO-GlcNAc transferaseOGT protein, humanProtein-Arginine N-MethyltransferasesUbiquitin Thiolesterase

Identifiers

PMID39715739
PMCPMC11666572

What Socratic 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 Socratic graph.