Evidence map›Paper›PMID 20040490›Full record

ArticleDevelopment (Cambridge, England)2010

Regulation of cortical contractility and spindle positioning by the protein phosphatase 6 PPH-6 in one-cell stage C. elegans embryos.

Katayoun Afshar, Michael E Werner, Yu Chung Tse, Michael Glotzer, Pierre Gönczy

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Development (Cambridge, England), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

32 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Functional Role of Protein Phosphatase-6 (Current medicinal chemistry · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Protein phosphatases in the regulation of mitosis.The Journal of cell biology · 2019
    Review
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Katayoun AfsharSwiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Swiss Federal Institute of Technology (EPFL), Lausanne CH-1015, Switzerland.
Michael E Werner
Yu Chung Tse
Michael Glotzer
Pierre Gönczy
University of Chicago · USÉcole Polytechnique Fédérale de Lausanne · CH

Funding

Positioning the Plane of Cell Division During CytokinesisR01GM085087 · NIGMS · UNIVERSITY OF CHICAGO · PI GLOTZER, MICHAEL A. · 2008 to 2018
$3.3M
NIGMS NIH HHS 1R01GM085087NIGMS NIH HHS R01 GM085087
6 · The paper itself

Abstract

Modulation of the microtubule and the actin cytoskeleton is crucial for proper cell division. Protein phosphorylation is known to be an important regulatory mechanism modulating these cytoskeletal networks. By contrast, there is a relative paucity of information regarding how protein phosphatases contribute to such modulation. Here, we characterize the requirements for protein phosphatase PPH-6 and its associated subunit SAPS-1 in one-cell stage C. elegans embryos. We establish that the complex of PPH-6 and SAPS-1 (PPH-6/SAPS-1) is required for contractility of the actomyosin network and proper spindle positioning. Our analysis demonstrates that PPH-6/SAPS-1 regulates the organization of cortical non-muscle myosin II (NMY-2). Accordingly, we uncover that PPH-6/SAPS-1 contributes to cytokinesis by stimulating actomyosin contractility. Furthermore, we demonstrate that PPH-6/SAPS-1 is required for the proper generation of pulling forces on spindle poles during anaphase. Our results indicate that this requirement is distinct from the role in organizing the cortical actomyosin network. Instead, we uncover that PPH-6/SAPS-1 contributes to the cortical localization of two positive regulators of pulling forces, GPR-1/2 and LIN-5. Our findings provide the first insights into the role of a member of the PP6 family of phosphatases in metazoan development.

Indexed as

Gene Expression Regulation, DevelopmentalAnaphaseAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCytokinesisCytoskeletonFluorescent Antibody Technique, IndirectImmunoprecipitationPhosphoprotein PhosphatasesSpindle ApparatusCaenorhabditis elegans ProteinsPhosphoprotein Phosphatasesprotein phosphatase 6

Identifiers

PMID20040490
PMCPMC2799158
OpenAlexW2094294983

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.