Evidence map›Paper›PMID 29669220›Full record

ArticleAmerican journal of physiology. Cell physiology2018

SUMOylation regulates germinal vesicle breakdown and the Akt/PKB pathway during mouse oocyte maturation.

Weber Beringui Feitosa, Patricia L Morris

Open access · bronzeAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. DPAGT1-Mediated ProteinAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Recent advances in mammalian reproductive biology.Science China. Life sciences · 2020
    Review
  11. Loss of the E2 SUMO-conjugating enzymeDevelopment (Cambridge, England) · 2019
    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

2 authors at 1 institution in 1 country.

Weber Beringui FeitosaCenter for Biomedical Research, Population Council , New York, New York.ORCID 0000-0002-7020-694X
Patricia L MorrisCenter for Biomedical Research, Population Council , New York, New York.
Population Council · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMOylation, a process of posttranslational modification of proteins by the small ubiquitin-related modifier (SUMO) family of proteins, is known to be involved in yeast and mammalian somatic cell-cycle regulation. However, the identities of the SUMO-modified oocyte targets are largely unknown and the functional role(s) for SUMOylation during mammalian oocyte maturation remains unclear. On the basis of studies in non-germline cells, protein kinase B/Akt is a potential SUMOylation target in the mouse oocyte, where it plays an essential role in cell-cycle resumption and progression during maturation. This study investigated the temporal patterns and prospective role(s) for interactions between SUMOylation and Akt serine-phosphorylation during oocyte meiotic resumption. Pharmacological inhibition of SUMOylation significantly decreased follicular fluid meiosis-activating sterol-induced cell-cycle resumption in oocytes matured in vitro and negatively affected the phosphorylation and nuclear translocation of Akt. Similarly, nuclear localization of cyclin D1, a downstream target of Akt activation, was significantly decreased following SUMOylation inhibition. Together these data show that SUMO and the posttranslational process of SUMOylation are involved in cell-cycle resumption during murine oocyte maturation and exert a regulatory influence on the Akt pathway during germinal vesicle breakdown.

Indexed as

AnimalsCell CycleCell NucleusCyclin D1FemaleGerminal CenterMiceOocytesPhosphorylationProtein Processing, Post-TranslationalProtein TransportProto-Oncogene Proteins c-aktSumoylationCyclin D1Proto-Oncogene Proteins c-aktcyclin D1FF-MASGVGVBDSUMO

Identifiers

PMID29669220
PMCPMC6087733
OpenAlexW2801148568

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.