Evidence map›Paper›PMID 9312014›Full record

ArticleThe EMBO journal1997

A member of the Ste20/PAK family of protein kinases is involved in both arrest of Xenopus oocytes at G2/prophase of the first meiotic cell cycle and in prevention of apoptosis.

S Faure, S Vigneron, M Dorée, N Morin

Abstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. PAK thread from amoeba to mammals.Journal of cellular biochemistry · 2009
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Regulation of the p21-activated kinase (PAK) by a human Gbeta -like WD-repeat protein, hPIP1.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  19. Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

4 authors.

S FaureCentre de Recherches de Biochimie Macromoléculaire, CNRS ERS 155, 1919 route de Mende, 34293 Montpellier Cedex 5, France.
S Vigneron
M Dorée
N Morin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have identified new members (X-PAKs) of the Ste20/PAK family of protein kinases in Xenopus, and investigated their role in the process that maintains oocytes arrested in the cell cycle. Microinjection of a catalytically inactive mutant of X-PAK1 with a K/R substitution in the ATP binding site, also deleted of its Nter-half that contains the conserved domains responsible for binding of both Cdc42/Rac GTPases and SH3-containing proteins, greatly facilitates oocyte release from G2/prophase arrest by progesterone and insulin. Addition of the same X-PAK1 mutant to cell cycle extracts from unfertilized eggs induced apoptosis, as shown by activation of caspases and cytological changes in in vitro-assembled nuclei. This was suppressed by adding Bcl-2 or the DEVD peptide inhibitor of caspases, and rescued by competing the dominant-negative mutant with its constitutively active X-PAK1 counterpart. Such results indicate that X-PAK1 (or another member of the Xenopus Ste20/PAK family of protein kinases) is involved in arrest of oocytes at G2/prophase and prevention of apoptosis; thus death by apoptosis and release of healthy oocytes from cell cycle arrest may be linked. That cell cycle arrest protects oocytes from apoptosis is consistent with the finding that extracts from metaphase II-arrested oocytes are less sensitive to apoptotic signals than those from activated eggs.

Indexed as

Saccharomyces cerevisiae ProteinsAdenosine TriphosphateAmino Acid SequenceAmino Acid SubstitutionAnimalsApoptosisBase SequenceBinding SitesCell CycleDNA PrimersFemaleG2 PhaseGuanosine 5'-O-(3-Thiotriphosphate)InsulinIntracellular Signaling Peptides and ProteinsKineticsAdenosine TriphosphateDNA PrimersGuanosine 5'-O-(3-Thiotriphosphate)InsulinIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesOligopeptidesp21-Activated KinasesProgesteroneProtein Serine-Threonine KinasesProto-Oncogene Proteins c-bcl-2Recombinant ProteinsSaccharomyces cerevisiae ProteinsSTE20 protein, S cerevisiae

Identifiers

PMID9312014
PMCPMC1170187

What OpenQuestion holds

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Registered trials

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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.