Evidence map›Paper›PMID 19889970›Full record

ArticleJournal of cell science2009

In vivo roles for Arp2/3 in cortical actin organization during C. elegans gastrulation.

Minna Roh-Johnson, Bob Goldstein

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. 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
0.8field-weighted citation impact, top 34% 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, 42 citations in OpenAlex.

  1. Article
  2. Asymmetric distribution of actin-related proteins in the earlybioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
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  10. Review
  11. Review
  12. Genetics · 2020
    Review
  13. Article
  14. The secreted MSP domain ofDevelopment (Cambridge, England) · 2017
    Article
  15. A GAP that Divides.F1000Research · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Actin-related protein2/3 complex regulates tight junctions and terminal differentiation to promote epidermal barrier formation.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

2 authors at 1 institution in 1 country.

Minna Roh-JohnsonBiology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. minna_roh@med.unc.edu
Bob Goldstein
University of North Carolina at Chapel Hill · US

Funding

Mechanisms of C. elegans GastrulationR01GM083071 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GOLDSTEIN, ROBERT P · 2008 to 2019
$3.7M
NIGMS NIH HHS R01 GM083071NIGMS NIH HHS R01-GM083071
6 · The paper itself

Abstract

The Arp2/3 complex is important for morphogenesis in various developmental systems, but specific in vivo roles for this complex in cells that move during morphogenesis are not well understood. We have examined cellular roles for Arp2/3 in the Caenorhabditis elegans embryo. In C. elegans, the first morphogenetic movement, gastrulation, is initiated by the internalization of two endodermal precursor cells. These cells undergo a myosin-dependent apical constriction, pulling a ring of six neighboring cells into a gap left behind on the ventral surface of the embryo. In agreement with a previous report, we found that in Arp2/3-depleted C. elegans embryos, membrane blebs form and the endodermal precursor cells fail to fully internalize. We show that these cells are normal with respect to several key requirements for gastrulation: cell cycle timing, cell fate, apicobasal cell polarity and apical accumulation and activation of myosin-II. To further understand the function of Arp2/3 in gastrulation, we examined F-actin dynamics in wild-type embryos. We found that three of the six neighboring cells extend short, dynamic F-actin-rich processes at their apical borders with the internalizing cells. These processes failed to form in embryos that were depleted of Arp2/3 or the apical protein PAR-3. Our results identify an in vivo role for Arp2/3 in the formation of subcellular structures during morphogenesis. The results also suggest a new layer to the model of C. elegans gastrulation: in addition to apical constriction, internalization of the endoderm might involve dynamic Arp2/3-dependent F-actin-rich extensions on one side of a ring of cells.

Indexed as

Cell PolarityGastrulationActin-Related Protein 2Actin-Related Protein 3ActinsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell LineageEmbryo, NonmammalianProtein BindingActin-Related Protein 2Actin-Related Protein 3Actinsarx-1 protein, C elegansarx-2 protein, C elegansCaenorhabditis elegans Proteins

Identifiers

PMID19889970
PMCPMC2773197
OpenAlexW2045374225

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.