Evidence map›Paper›PMID 19879842›Full record

ArticleCell2009

Regulation of MBK-2/DYRK by CDK-1 and the pseudophosphatases EGG-4 and EGG-5 during the oocyte-to-embryo transition.

Ken Chih-Chien Cheng, Richard Klancer, Andrew Singson, Geraldine Seydoux

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

54 citing papers in PubMed, 110 citations in OpenAlex.

  1. Article
  2. A mechanism for MEX-5-driven disassembly of PGL-3/RNA condensates in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Understanding Pseudophosphatase Function Through Biochemical Interactions.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Article
  6. Article
  7. Pseudophosphatases as Regulators of MAPK Signaling.International journal of molecular sciences · 2021
    Review
  8. Article
  9. The Roles of Pseudophosphatases in Disease.International journal of molecular sciences · 2021
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. PLK-1 Regulation of Asymmetric Cell Division in the EarlyFrontiers in cell and developmental biology · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Ken Chih-Chien ChengDepartment of Molecular Biology and Genetics and Howard Hughes Medical Institute, Center for Cell Dynamics, Johns Hopkins School of Medicine, 725 N. Wolfe Street, PCTB 706, Baltimore, MD 21205, USA.
Richard Klancer
Andrew Singson
Geraldine Seydoux
Howard Hughes Medical Institute · USRutgers, The State University of New Jersey · US

Funding

[RNW] - Gamete Interactions in Caenorhabditis elegansR01HD054681 · NICHD · RUTGERS, THE STATE UNIV OF N.J. · PI ANDREW W. SINGSON · 2008 to 2026
$5.3M
REGULATION OF GERM CELL FATE DURING EMBRYOGENESISR01HD037047 · NICHD · JOHNS HOPKINS UNIVERSITY · PI GERALDINE Catherine Joelle SEYDOUX · 1999 to 2026
$4.3M
Howard Hughes Medical InstituteNICHD NIH HHS R01 HD037047NICHD NIH HHS R01 HD054681NICHD NIH HHS R01HD054681NICHD NIH HHS R01HD37047
6 · The paper itself

Abstract

DYRKs are kinases that self-activate in vitro by autophosphorylation of a YTY motif in the kinase domain, but their regulation in vivo is not well understood. In C. elegans zygotes, MBK-2/DYRK phosphorylates oocyte proteins at the end of the meiotic divisions to promote the oocyte-to-embryo transition. Here we demonstrate that MBK-2 is under both positive and negative regulation during the transition. MBK-2 is activated during oocyte maturation by CDK-1-dependent phosphorylation of serine 68, a residue outside of the kinase domain required for full activity in vivo. The pseudotyrosine phosphatases EGG-4 and EGG-5 sequester activated MBK-2 until the meiotic divisions by binding to the YTY motif and inhibiting MBK-2's kinase activity directly, using a mixed-inhibition mechanism that does not involve tyrosine dephosphorylation. Our findings link cell-cycle progression to MBK-2/DYRK activation and the oocyte-to-embryo transition.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCDC2 Protein KinaseEmbryo, NonmammalianHumansOocytesProtein-Tyrosine KinasesCaenorhabditis elegans ProteinsCDC2 Protein KinaseEGG-4 protein, C elegansEGG-5 protein, C elegansMBK-2 protein, C elegansProtein-Tyrosine Kinases

Identifiers

PMID19879842
PMCPMC2790168
OpenAlexW2142803231

What OpenQuestion holds

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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.