Evidence map›Paper›PMID 12477927›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

G2 arrest in Xenopus oocytes depends on phosphorylation of cdc25 by protein kinase A.

Brian C Duckworth, Jennifer S Weaver, Joan V Ruderman

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
14.9field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 205 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. TheBiomolecules · 2025
    Review
  5. Egg Overactivation-An Overlooked Phenomenon of Gamete Physiology.International journal of molecular sciences · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Regulation of oocyte maturation: Role of conserved ERK signaling.Molecular reproduction and development · 2022
    Review
  12. Article
  13. Review
  14. Review
  15. Dissection of the Ovulatory Process UsingFrontiers in cell and developmental biology · 2020
    Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Brian C DuckworthDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Jennifer S Weaver
Joan V Ruderman
Harvard University · US

Funding

Cell Adhesion Molecules of Mammalian FertilizationR01HD037696 · NICHD · JOHNS HOPKINS UNIVERSITY · PI EVANS, JANICE P · 2004 to 2008
$1.8M
CELL ADHESION MOLECULES OF MAMMALIAN FERTILIZATIONR29HD037696 · NICHD · JOHNS HOPKINS UNIVERSITY · PI EVANS, JANICE P · 1998 to 2002
$347k
NICHD NIH HHS HD37696NICHD NIH HHS R01 HD037696NICHD NIH HHS R29 HD037696
6 · The paper itself

Abstract

Xenopus oocytes, which are arrested in G(2) of meiosis I, contain complexes of cyclin B-cdc2 (M phase-promoting factor) that are kept repressed by inhibitory phosphorylations on cdc2 at Thr-14 and Tyr-15. Progesterone induces a cytoplasmic signaling pathway that leads to activation of cdc25, the phosphatase that removes these phosphorylations, catalyzing entry into M phase. It has been known for 25 years that high levels of cAMP and protein kinase A (PKA) are required to maintain the G(2) arrest and that a drop in PKA activity is required for M phase-promoting factor activation, but no physiological targets of PKA have been identified. We present evidence that cdc25 is a critical target of PKA. (i) In vitro, cdc25 Ser-287 serves as a major site of phosphorylation by PKA, resulting in sequestration by 14-3-3. (ii) Endogenous cdc25 is phosphorylated on Ser-287 in oocytes and dephosphorylated in response to progesterone just before cdc2 dephosphorylation and M-phase entry. (iii) High PKA activity maintains phosphorylation of Ser-287 in vivo, whereas inhibition of PKA by its heat-stable inhibitor (PKI) induces dephosphorylation of Ser-287. (iv) Overexpression of mutant cdc25 (S287A) bypasses the ability of PKA to maintain oocytes in G(2) arrest. These findings argue that cdc25 is a physiologically relevant target of PKA in oocytes. In the early embryonic cell cycles, Ser-287 is phosphorylated during interphase and dephosphorylated just before cdc2 activation and mitotic entry. Thus, in addition to its role in checkpoint arrest, cdc25 Ser-287 serves as a site for regulation during normal, unperturbed cell cycles.

Indexed as

G2 PhaseAnimalscdc25 PhosphatasesCyclic AMPCyclic AMP-Dependent Protein KinasesEnzyme ActivationFemaleMitogen-Activated Protein KinasesOocytesPhosphorylationProgesteroneXenopuscdc25 PhosphatasesCyclic AMPCyclic AMP-Dependent Protein KinasesMitogen-Activated Protein KinasesProgesterone

Identifiers

PMID12477927
PMCPMC139223
OpenAlexW2039144927

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.