Evidence map›Paper›PMID 23264738›Full record

ArticleJournal of cell science2013

PtdIns(3,4,5)P3 is constitutively synthesized and required for spindle translocation during meiosis in mouse oocytes.

Ping Zheng, Boris Baibakov, Xi-hong Wang, Jurrien Dean

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Advances in the study of CDC42 in the female reproductive system.Journal of cellular and molecular medicine · 2022
    Review
  7. Article
  8. Article
  9. Dissecting the mechanisms of cell division.The Journal of biological chemistry · 2019
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Symmetry breaking and polarity establishment during mouse oocyte maturation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    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 at 3 institutions in 2 countries.

Ping ZhengState Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China. zhengp@mail.kiz.ac.cn
Boris Baibakov
Xi-hong Wang
Jurrien Dean
Chinese Academy of Sciences · CNNational Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Molecular Biology of the OocyteZIADK015603 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI DEAN, JURRIEN · 2009 to 2025
$43.2M
Intramural NIH HHS
6 · The paper itself

Abstract

Prior to ovulation, mammalian oocytes complete their first meiotic division and arrest at metaphase II. During this marked asymmetric cell division, the meiotic spindle moves dramatically from the center of the oocyte to the cortex to facilitate segregation of half of its chromosomal content into the diminutive first polar body. Recent investigations have documented crucial roles for filamentous actin (F-actin) in meiotic spindle translocation. However, the identity of the upstream regulators responsible for these carefully orchestrated movements has remained elusive. Utilizing fluorescently tagged probes and time-lapse confocal microscopy, we document that phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] is constitutively synthesized with spatial and temporal dynamics similar to that of F-actin and Formin 2 (Fmn2). Blockage of PtdIns(3,4,5)P3 synthesis by LY294002, a specific inhibitor of phosphoinositide 3-kinase (PI3K), disrupts cytoplasmic F-actin organization and meiotic spindle migration to the cortex. F-actin nucleator Fmn2 and Rho GTPase Cdc42 play roles in mediating the effect of PtdIns(3,4,5)P3 on F-actin assembly. Moreover, the spatial and temporal dynamics of PtdIns(3,4,5)P3 is impaired by depletion of MATER or Filia, two oocyte proteins encoded by maternal effect genes. Thus, PtdIns(3,4,5)P3 is synthesized during meiotic maturation and acts upstream of Cdc42 and Fmn2, but downstream of MATER/Filia proteins to regulate the F-actin organization and spindle translocation to the cortex during mouse oocyte meiosis.

Indexed as

ActinsAnimalsAntigenscdc42 GTP-Binding ProteinCells, CulturedChromonesEgg ProteinsFemaleForminsMeiosisMiceMice, Inbred C57BLMicrofilament ProteinsMicroscopy, ConfocalMorpholinesM Phase Cell Cycle Checkpoints2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneActinsAntigenscdc42 GTP-Binding ProteinChromonesEgg Proteinsfilia protein, mouseformin 2 protein, mouseForminsMicrofilament ProteinsMorpholinesNalp5 protein, mouseNerve Tissue ProteinsNuclear Proteinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoinositide-3 Kinase InhibitorsProteins

Identifiers

PMID23264738
PMCPMC3619807
OpenAlexW2104339463

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.