Evidence map›Paper›PMID 20543581›Full record

ArticleCell cycle (Georgetown, Tex.)2010

The SUMO pathway functions in mouse oocyte maturation.

Zhen-Bo Wang, Xiang-Hong Ou, Jing-Shan Tong, Sen Li, Liang Wei, Ying-Chun Ouyang, Yi Hou, Heide Schatten, Qing-Yuan Sun

Open access · hybridAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

30 citing papers in PubMed, 47 citations in OpenAlex.

  1. Molecular mechanisms of folliculogenesis and oogenesis.Systems biology in reproductive medicine · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Particulate matter-induced epigenetic modifications and lung complications.European respiratory review : an official journal of the European Respiratory Society · 2024
    Review
  7. Review
  8. Sumoylation regulates functional properties of the oocyte transcription factors SOHLH1 and NOBOX.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  9. Article
  10. Article
  11. Review
  12. Mechanisms of Oocyte Maturation and Related Epigenetic Regulation.Frontiers in cell and developmental biology · 2021
    Review
  13. DPAGT1-Mediated ProteinAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  14. The role of SUMOylation during development.Biochemical Society transactions · 2020
    Review
  15. Recent advances in mammalian reproductive biology.Science China. Life sciences · 2020
    Review
  16. Loss of the E2 SUMO-conjugating enzymeDevelopment (Cambridge, England) · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Cross-talk between sumoylation and phosphorylation in mouse spermatocytes.Biochemical and biophysical research communications · 2017
    Article
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

9 authors at 2 institutions in 2 countries.

Zhen-Bo WangState Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China.
Xiang-Hong Ou
Jing-Shan Tong
Sen Li
Liang Wei
Ying-Chun Ouyang
Yi Hou
Heide Schatten
Qing-Yuan Sun
Chinese Academy of Sciences · CNNational Council for Scientific and Technological Development · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sumoylation is an important post-translational modification in which SUMO (small ubiquitin-related modifier) proteins are bonded covalently to their substrates. Studies on the roles of sumoylation in cell cycle regulation have been emerging in both mitosis from yeast to mammals and meiosis in budding yeast, but the functions of sumoylation in mammalian meiosis, especially in oocyte meiotic maturation are not well known. Here, we examined the localization and expression of SUMO-1 and SUMO-2/3, the two basic proteins in the sumoylation pathway and investigated their roles through over-expression of Senp2 during mouse oocyte maturation. Immunofluorescent staining revealed differential patterns of SUMO-1 and SUMO-2/3 localization: SUMO-1 was localized to the spindle poles in prometaphase I, MI and MII stages, around the separating homologues in anaphase I and telophase I stages of first meiosis, while SUMO-2/3 was mainly concentrated near centromeres during mouse oocyte maturation. Immunoblot analysis uncovered the different expression profiles of SUMO-1 and SUMO-2/3 modified proteins during mouse oocyte maturation. Over-expression of Senp2, a SUMO-specific isopeptidase, caused changes of SUMO-modified proteins and led to defects in MII spindle organization in mature eggs. These results suggest that the SUMO pathway may play an indispensable role during mouse oocyte meiotic maturation.

Indexed as

Cell DifferentiationSignal TransductionAnimalsCysteine EndopeptidasesFemaleGene Expression ProfilingMeiosisMiceMultienzyme ComplexesOocytesProtein TransportSmall Ubiquitin-Related Modifier ProteinsSpindle ApparatusSubcellular FractionsSumoylationTime FactorsCysteine EndopeptidasesMultienzyme ComplexesSenp2 protein, mouseSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID20543581
PMCPMC3322456
OpenAlexW2093546609

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.