Evidence map›Paper›PMID 20948319›Full record

ArticleCell cycle (Georgetown, Tex.)2010

p38α MAPK is a MTOC-associated protein regulating spindle assembly, spindle length and accurate chromosome segregation during mouse oocyte meiotic maturation.

Xiang-Hong Ou, Sen Li, Bao-Zeng Xu, Zhen-Bo Wang, Song Quan, Mo Li, Qing-Hua Zhang, Ying-Chun Ouyang, Heide Schatten, Fu-Qi Xing and 1 more

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. PKCβ1 regulates meiotic cell cycle in mouse oocyte.Cell cycle (Georgetown, Tex.) · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Heme oxygenase/carbon monoxide in the female reproductive system: an overlooked signalling pathway.International journal of biochemistry and molecular biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 9 institutions in 3 countries.

Xiang-Hong OuCenter of Reproductive Medicine, Department of Obstetrics and Gynecology, Nanfang Hospital, Southern Medical University, Guangzhou, China.
Sen Li
Bao-Zeng Xu
Zhen-Bo Wang
Song Quan
Mo Li
Qing-Hua Zhang
Ying-Chun Ouyang
Heide Schatten
Fu-Qi Xing
Qing-Yuan Sun
Chinese Academy of Sciences · CNChinese Academy of Social Sciences · CNGuangzhou Experimental Station · CNInstitute of Zoology · CNInstitute of Zoology · KZJingdong (China) · CNNanfang Hospital · CNSouthern Medical University · CNUniversity of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P38αMAPK (p38α) is usually activated in response to various stresses and plays a role in the inhibition of cell proliferation and tumor progression, but little is known about its roles in meiotic spindle assembly. In this study, we characterized the dynamic localization of p38α and explored its function in mouse oocyte meiotic maturation. P38α specifically colocalized with γ-tubulin and Plk1 at the center of MTOCs and spindle poles. Depletion of p38α by specific morpholino injection resulted in severely defective spindles and misaligned chromosomes probably via MK2 dephosphorylation. Notably, depletion of p38α led to significant spindle pole defects, spindle elongation, non-tethered kinetochore microtubules and increased microtubule tension. The disruption of spindle stability was coupled with decreased γ-tubulin and Plk1 at MTOCs. Overexpression of Eg5, a conserved motor protein, also caused spindle elongation and its morpholino injection almost completely rescued spindle elongation caused by p38α depletion. In addition, p38α-depletion decreased BubR1 and interfered with spindle assembly checkpoint (SAC), which resulted in aneuploid oocytes. Together, these data indicate that p38α is an important component of MTOCs, which regulates spindle assembly and spindle length, as well as stabilizes the spindle and spindle poles. Perturbed SAC and abnormal microtubule tension may be responsible for the misaligned chromosomes and high aneuploidy in p38α-depleted mouse oocytes.

Indexed as

Chromosome SegregationOocytesAneuploidyAnimalsGene SilencingIntracellular Signaling Peptides and ProteinsKinesinsMAP-Kinase-Activated Kinase 2MeiosisMiceMicrotubule-Organizing CenterMicrotubulesMitogen-Activated Protein Kinase 14Protein Serine-Threonine KinasesSpindle ApparatusTubulinIntracellular Signaling Peptides and ProteinsKIF11 protein, humanKinesinsMAP-Kinase-Activated Kinase 2Mitogen-Activated Protein Kinase 14Protein Serine-Threonine KinasesTubulin

Identifiers

PMID20948319
PMCPMC3055197
OpenAlexW2005131330

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.