Evidence map›Paper›PMID 17881560›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A.

Judy Qiju Wu, David V Hansen, Yanxiang Guo, Michael Zhuo Wang, Wanli Tang, Christopher D Freel, Jeffrey J Tung, Peter K Jackson, Sally Kornbluth

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Vertebrate Reproduction.Cold Spring Harbor perspectives in biology · 2015
    Review
  6. Article
  7. Article
  8. Suppression of DNA-damage checkpoint signaling by Rsk-mediated phosphorylation of Mre11.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  9. Article
  10. Article
  11. Review
  12. Pioneering the Xenopus oocyte and egg extract system.The Journal of biological chemistry · 2012
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  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

9 authors at 4 institutions in 1 country.

Judy Qiju WuDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
David V Hansen
Yanxiang Guo
Michael Zhuo Wang
Wanli Tang
Christopher D Freel
Jeffrey J Tung
Peter K Jackson
Sally Kornbluth
Duke Medical Center · USDuke University Hospital · USStanford University · USUniversity of North Carolina at Chapel Hill · US

Funding

Control of Mitotic Entry by Regulators of Cdc2R01GM067225 · NIGMS · DUKE UNIVERSITY · PI KORNBLUTH, SALLY A · 2003 to 2010
$2.1M
Proteolytic Control of Early Events in MitosisR01GM073023 · NIGMS · STANFORD UNIVERSITY · PI FERRELL, JAMES E. · 2005 to 2008
$1.1M
NIGMS NIH HHS R01 GM067225NIGMS NIH HHS R01 GM073023NIGMS NIH HHS R01 GM67225
6 · The paper itself

Abstract

Before fertilization, vertebrate eggs are arrested in meiosis II by cytostatic factor (CSF), which holds the anaphase-promoting complex (APC) in an inactive state. It was recently reported that Mos, an integral component of CSF, acts in part by promoting the Rsk-mediated phosphorylation of the APC inhibitor Emi2/Erp1. We report here that Rsk phosphorylation of Emi2 promotes its interaction with the protein phosphatase PP2A. Emi2 residues adjacent to the Rsk phosphorylation site were important for PP2A binding. An Emi2 mutant that retained Rsk phosphorylation but lacked PP2A binding could not be modulated by Mos. PP2A bound to Emi2 acted on two distinct clusters of sites phosphorylated by Cdc2, one responsible for modulating its stability during CSF arrest and one that controls binding to the APC. These findings provide a molecular mechanism for Mos action in promoting CSF arrest and also define an unusual mechanism, whereby protein phosphorylation recruits a phosphatase for dephosphorylation of distinct sites phosphorylated by another kinase.

Indexed as

MeiosisAmino Acid SequenceAnimalsF-Box ProteinsHumansMolecular Sequence DataOvumPhosphorylase PhosphatasePhosphorylationProto-Oncogene Proteins c-mosRibosomal Protein S6 KinasesSignal TransductionXenopusXenopus ProteinsF-Box ProteinsFBXO43 protein, XenopusMos protein, XenopusPhosphorylase PhosphataseProto-Oncogene Proteins c-mosRibosomal Protein S6 KinasesXenopus Proteins

Identifiers

PMID17881560
PMCPMC2034268
OpenAlexW2066730352

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.