Evidence map›Paper›PMID 23424200›Full record

ArticleJournal of cell science2013

Mechanisms of CDC-42 activation during contact-induced cell polarization.

Emily Chan, Jeremy Nance

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. LGL-1 and the RhoGAP protein PAC-1 redundantly polarize thebioRxiv : the preprint server for biology · 2026
    Article
  2. The actin assembly regulatorbioRxiv : the preprint server for biology · 2025
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  3. Article
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  5. Origin and development of primary animal epithelia.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Computational study of biomechanical drivers of renal cystogenesis.Biomechanics and modeling in mechanobiology · 2023
    Article
  10. Article
  11. Apical PAR-3 caps orient the mitotic spindle inbioRxiv : the preprint server for biology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Genetics · 2020
    Review
  16. TheGenetics · 2019
    Review
  17. Planar Asymmetries in theFrontiers in cell and developmental biology · 2019
    Article
  18. Article
  19. Article
  20. Review
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.

Emily ChanHelen L. and Martin S. Kimmel Center for Biology and Medicine at the Skirball Institute of Biomolecular Medicine, NYU School of Medicine, New York, NY 10016, USA.
Jeremy Nance
New York University · US

Funding

Mechanisms of Contact-Mediated Cell Polarization in the C. elegans Embryo.R01GM078341 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI NANCE, JEREMY · 2007 to 2015
$3.1M
NIGMS NIH HHS R01 GM078341
6 · The paper itself

Abstract

Polarization of early embryos provides a foundation to execute essential patterning and morphogenetic events. In Caenorhabditis elegans, cell contacts polarize early embryos along their radial axis by excluding the cortical polarity protein PAR-6 from sites of cell contact, thereby restricting PAR-6 to contact-free cell surfaces. Radial polarization requires the cortically enriched Rho GTPase CDC-42, which in its active form recruits PAR-6 through direct binding. The Rho GTPase activating protein (RhoGAP) PAC-1, which localizes specifically to cell contacts, triggers radial polarization by inactivating CDC-42 at these sites. The mechanisms responsible for activating CDC-42 at contact-free surfaces are unknown. Here, in an overexpression screen of Rho guanine nucleotide exchange factors (RhoGEFs), which can activate Rho GTPases, we identify CGEF-1 and ECT-2 as RhoGEFs that act through CDC-42 to recruit PAR-6 to the cortex. We show that ECT-2 and CGEF-1 localize to the cell surface and that removing their activity causes a reduction in levels of cortical PAR-6. Through a structure-function analysis, we show that the tandem DH-PH domains of CGEF-1 and ECT-2 are sufficient for GEF activity, but that regions outside of these domains target each protein to the cell surface. Finally, we provide evidence suggesting that the N-terminal region of ECT-2 may direct its in vivo preference for CDC-42 over another known target, the Rho GTPase RHO-1. We propose that radial polarization results from a competition between RhoGEFs, which activate CDC-42 throughout the cortex, and the RhoGAP PAC-1, which inactivates CDC-42 at cell contacts.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans Proteinscdc42 GTP-Binding ProteinCell PolarityGuanine Nucleotide Exchange FactorsRho Guanine Nucleotide Exchange FactorsCaenorhabditis elegans Proteinscdc42 GTP-Binding ProteinEct-2 protein, C elegansGuanine Nucleotide Exchange FactorsRho Guanine Nucleotide Exchange FactorsCaenorhabditis elegansCDC-42Cell polarityECT-2RhoGEF

Identifiers

PMID23424200
PMCPMC3647442
OpenAlexW2167408228

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.