Evidence map›Paper›PMID 39944690›Full record

ReviewFrontiers in immunology2025

Emerging roles of mitochondrial sirtuin SIRT5 in succinylation modification and cancer development.

Zhangmin Ke, Kaikai Shen, Li Wang, Hao Xu, Xia Pan, Zhenjue Qian, Yuting Wen, Tangfeng Lv, Xiuwei Zhang, Yong Song

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
  2. Aspirin-Derived Salicyl-CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Mitochondrial metabolism and cancer therapeutic innovation.Signal transduction and targeted therapy · 2025
    Review
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

10 authors.

Zhangmin Ke *Department of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Kaikai Shen *Department of Respiratory and Critical Care Medicine, Jinling Hospital, Affiliated Hospital of Medical School, Nanjing University, Nanjing, China.
Li WangDepartment of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Hao XuDepartment of Respiratory and Critical Care Medicine, The People's Hospital of Danyang, Affiliated Danyang Hospital of Nantong University, Zhenjiang, China.
Xia PanDepartment of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Zhenjue QianDepartment of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Yuting WenDepartment of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Tangfeng LvDepartment of Respiratory and Critical Care Medicine, Jinling Hospital, Nanjing Medical University, Nanjing, China.
Xiuwei ZhangDepartment of Respiratory and Critical Care Medicine, Affiliated Jiangning Hospital of Nanjing Medicine University, Nanjing, China.
Yong SongDepartment of Respiratory and Critical Care Medicine, Jinling Hospital, Nanjing Medical University, Nanjing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Succinylation represents an emerging class of post-translational modifications (PTMs), characterized by the enzymatic or non-enzymatic transfer of a negatively charged four-carbon succinyl group to the ϵ-amino group of lysine residues, mediated by succinyl-coenzyme A. Recent studies have highlighted the involvement of succinylation in various diseases, particularly cancer progression. Sirtuin 5 (SIRT5), a member of the sirtuin family, has been extensively studied for its robust desuccinylase activity, alongside its deacetylase function. To date, only a limited number of SIRT5 substrates have been identified. These substrates mediate diverse physiological processes such as glucose oxidation, fatty acid oxidation, ammonia detoxification, reactive oxygen species scavenging, anti-apoptosis, and inflammatory responses. The regulation of these activities can occur through either the same enzymatic activity acting on different substrates or distinct enzymatic activities targeting the same substrate. Aberrant expression of SIRT5 has been closely linked to tumorigenesis and disease progression; however, its role remains controversial. SIRT5 exhibits dual functionalities: it can promote tumor proliferation, metastasis, drug resistance, and metabolic reprogramming, thereby acting as an oncogene; conversely, it can also inhibit tumor cell growth and induce apoptosis, functioning as a tumor suppressor gene. This review aims to provide a comprehensive overview of the current research status of SIRT5. We discuss its structural characteristics and regulatory mechanisms, compare its functions with other sirtuin family members, and elucidate the mechanisms regulating SIRT5 activity. Specifically, we focus on the role of succinylation modification mediated by SIRT5 in tumor progression, highlighting how desuccinylation by SIRT5 modulates tumor development and delineating the underlying mechanisms involved.

Indexed as

MitochondriaNeoplasmsProtein Processing, Post-TranslationalSirtuinsSuccinic AcidAnimalsHumansSIRT5 protein, humanSirtuinsSuccinic AcidcancerdesuccinylaseSIRT5sirtuinsuccinylation

Identifiers

PMID39944690
PMCPMC11814216

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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.