Evidence map›Paper›PMID 39438456›Full record

ArticleCell death discovery2024

Mutation of the SUMOylation site of Aurora-B disrupts spindle formation and chromosome alignment in oocytes.

Shan-Shan Chen, Li Li, Bo Yao, Jia-Lun Guo, Ping-Shuang Lu, Hao-Lin Zhang, Kun-Huan Zhang, Yuan-Jing Zou, Nan-Jian Luo, Shao-Chen Sun and 2 more

Abstract read
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Article in Cell death discovery, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
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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.

Shan-Shan ChenDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Li LiDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Bo YaoDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Jia-Lun GuoDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Ping-Shuang LuCollege of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Hao-Lin ZhangCollege of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Kun-Huan ZhangCollege of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Yuan-Jing ZouCollege of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Nan-Jian LuoDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China.
Shao-Chen SunCollege of Animal Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu, 210095, China.
Lin-Lin HuKey Laboratory of Research on Clinical Molecular Diagnosis for High Incidence Diseases in Western Guangxi, Affiliated Hospital of Youjiang Medical University for Nationalities, Baise, Guangxi, 533000, China. hutwolin@126.com.
Yan-Ping RenDepartment of Histology and Embryology, School of Preclinical Medicine, Zunyi Medical University, Zunyi, Guizhou, 563000, China. ypren@zmu.edu.cn.ORCID http://orcid.org/0000-0002-0269-1656

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aurora-B is a kinase that regulates spindle assembly and kinetochore-microtubule (KT-MT) attachment during mitosis and meiosis. SUMOylation is involved in the oocyte meiosis regulation through promoting spindle assembly and chromosome segregation, but its substrates to support this function is still unknown. It is reported that Aurora-B is SUMOylated in somatic cells, and SUMOylated Aurora-B contributes the process of mitosis. However, whether Aurora-B is SUMOylated in oocytes and how SUMOylation of Aurora-B impacts its function in oocyte meiosis remain poorly understood. In this study, we report that Aurora-B is modified by SUMOylation in mouse oocytes. The results show that Aurora-B colocalized and interacted with SUMO-2/3 in mouse oocytes, confirming that Aurora-B is modified by SUMO-2/3 in this system. Compared with that in young mice, the protein expression of SUMO-2/3 decreased in the oocytes of aged mice, indicating that SUMOylation might be related to mouse aging. Overexpression of Aurora-B SUMOylation site mutants, Aurora-B

Identifiers

PMID39438456
PMCPMC11496499

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.