Evidence map›Paper›PMID 39127633›Full record

ReviewCellular & molecular biology letters2024

Crosstalk between SUMOylation and other post-translational modifications in breast cancer.

Bajin Wei, Fan Yang, Luyang Yu, Cong Qiu

Abstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Vitiligo Information Resource database v3.NPJ systems biology and applications · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Article
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  12. Article
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  15. Article
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  17. Article
  18. Article
  19. Ubiquitination in cancer: mechanisms and therapeutic opportunities.Cancer communications (London, England) · 2025
    Review
  20. 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

4 authors.

Bajin Wei *The Department of Breast Surgery, Key Laboratory of Organ Transplantation, Key Laboratory of Combined Multi-Organ Transplantation, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.
Fan Yang *State Key Laboratory for Diagnosis and Treatment of Infectious Diseases, National Clinical Research Center for Infectious Diseases, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, Hangzhou, China.
Luyang YuMOE Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences, Zijingang Campus, Zhejiang University, No. 866 Yuhangtang Road, Hangzhou, 310058, Zhejiang, China. luyangyu@zju.edu.cn.
Cong QiuMOE Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences, Zijingang Campus, Zhejiang University, No. 866 Yuhangtang Road, Hangzhou, 310058, Zhejiang, China. congqiu@zju.edu.cn.ORCID http://orcid.org/0000-0002-0527-8824

Funding

National Key Research and Development Program of China 2018YFA0800504National Key Research and Development Program of China 2021YFA1101100National Natural Science Foundation of China 81970372
6 · The paper itself

Abstract

Breast cancer represents the most prevalent tumor type and a foremost cause of mortality among women globally. The complex pathophysiological processes of breast cancer tumorigenesis and progression are regulated by protein post-translational modifications (PTMs), which are triggered by different carcinogenic factors and signaling pathways, with small ubiquitin-like modifier (SUMOylation) emerging as a particularly pivotal player in this context. Recent studies have demonstrated that SUMOylation does not act alone, but interacts with other PTMs, such as phosphorylation, ubiquitination, acetylation, and methylation, thereby leading to the regulation of various pathological activities in breast cancer. This review explores novel and existing mechanisms of crosstalk between SUMOylation and other PTMs. Typically, SUMOylation is regulated by phosphorylation to exert feedback control, while also modulates subsequent ubiquitination, acetylation, or methylation. The crosstalk pairs in promoting or inhibiting breast cancer are protein-specific and site-specific. In mechanism, alterations in amino acid side chain charges, protein conformations, or the occupation of specific sites at specific domains or sites underlie the complex crosstalk. In summary, this review centers on elucidating the crosstalk between SUMOylation and other PTMs in breast cancer oncogenesis and progression and discuss the molecular mechanisms contributing to these interactions, offering insights into their potential applications in facilitating novel treatments for breast cancer.

Indexed as

Breast NeoplasmsProtein Processing, Post-TranslationalSumoylationAcetylationAnimalsFemaleHumansMethylationPhosphorylationSignal TransductionUbiquitinationBreast cancerCrosstalkPost-translational modificationsSUMOylation

Identifiers

PMID39127633
PMCPMC11316377

What Socratic holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.