Evidence map›Paper›PMID 37904651›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2023

SUCLG2 Regulates Mitochondrial Dysfunction through Succinylation in Lung Adenocarcinoma.

Qifan Hu, Jing Xu, Lei Wang, Yi Yuan, Ruiguang Luo, Mingxi Gan, Keru Wang, Tao Zhao, Yawen Wang, Tianyu Han and 1 more

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

57 citing papers in PubMed, 68 citations in OpenAlex.

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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

11 authors at 1 institution in 1 country.

Qifan HuDepartment of Thoracic Surgery, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, 330006, China.
Jing XuSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Lei WangSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Yi YuanSchool of Huankui Academy, Nanchang University, Nanchang, Jiangxi, 330031, China.
Ruiguang LuoSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Mingxi GanSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Keru WangSchool of Huankui Academy, Nanchang University, Nanchang, Jiangxi, 330031, China.
Tao ZhaoSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Yawen WangSchool of Basic Medical Sciences, Nanchang University, Nanchang, Jiangxi, 330031, China.
Tianyu HanJiangxi Institute of Respiratory Disease, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, 330006, China.
Jian-Bin WangDepartment of Thoracic Surgery, The First Affiliated Hospital of Nanchang University, Nanchang, Jiangxi, 330006, China.ORCID 0000-0002-4706-1658
Nanchang University · CN

Funding

Nanchang University YQ202104National Natural Science Foundation of China 81902346National Natural Science Foundation of China 82030086National Natural Science Foundation of China 82273258Natural Science Foundation of Jiangxi Province 20212ACB216007Science and Technology Innovation High-end Talent Project of Jiangxi Province jxsq2023201100
6 · The paper itself

Abstract

Mitochondrial dysfunction and abnormal energy metabolism are major features of cancer. However, the mechanisms underlying mitochondrial dysfunction during cancer progression are far from being clarified. Here, it is demonstrated that the expression level of succinyl-coenzyme A (CoA) synthetase GDP-forming subunit β (SUCLG2) can affect the overall succinylation of lung adenocarcinoma (LUAD) cells. Succinylome analysis shows that the deletion of SUCLG2 can upregulate the succinylation level of mitochondrial proteins and inhibits the function of key metabolic enzymes by reducing either enzymatic activity or protein stability, thus dampening mitochondrial function in LUAD cells. Interestingly, SUCLG2 itself is also succinylated on Lys93, and this succinylation enhances its protein stability, leading to the upregulation of SUCLG2 and promoting the proliferation and tumorigenesis of LUAD cells. Sirtuin 5 (SIRT5) desuccinylates SUCLG2 on Lys93, followed by tripartite motif-containing protein 21 (TRIM21)-mediated ubiquitination through K63-linkage and degradation in the lysosome. The findings reveal a new role for SUCLG2 in mitochondrial dysfunction and clarify the mechanism of the succinylation-mediated protein homeostasis of SUCLG2 in LUAD, thus providing a theoretical basis for developing anti-cancer drugs targeting SUCLG2.

Indexed as

Adenocarcinoma of LungMitochondrial DiseasesHumansMitochondriamitochondrial dysfunctionSIRT5succinylationSUCLG2TRIM21

Identifiers

PMID37904651
PMCPMC10724390
OpenAlexW4388033551

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.