Evidence map›Paper›PMID 25452388›Full record

ArticleThe Journal of cell biology2014

An Elmo-Dock complex locally controls Rho GTPases and actin remodeling during cadherin-mediated adhesion.

Christopher P Toret, Caitlin Collins, W James Nelson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.3field-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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. Targeting of ELMO2 by thebioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. E-Cadherin: A conductor of cellular signaling.Current opinion in cell biology · 2025
    Review
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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

3 authors at 1 institution in 1 country.

Christopher P ToretDepartment of Biology; and Department of Molecular and Cellular Physiology, Stanford University School of Medicine; Stanford University, Stanford, CA 94305 christopher.TORET@univ-amu.fr wjnelson@stanford.edu.
Caitlin CollinsDepartment of Biology; and Department of Molecular and Cellular Physiology, Stanford University School of Medicine; Stanford University, Stanford, CA 94305.
W James NelsonDepartment of Biology; and Department of Molecular and Cellular Physiology, Stanford University School of Medicine; Stanford University, Stanford, CA 94305 Department of Biology; and Department of Molecular and Cellular Physiology, Stanford University School of Medicine; Stanford University, Stanford, CA 94305 christopher.TORET@univ-amu.fr wjnelson@stanford.edu.
Stanford University · US

Funding

Topogenesis of NA/K-ATPASE in Polarized Epithelial CellsR37GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 2003 to 2012
$7.4M
TUMOR BIOLOGYT32CA009151 · NCI · STANFORD UNIVERSITY · PI CLEARY, MICHAEL L · 1985 to 2014
$5.5M
Topogenesis of Na/K-ATPase in Polarized MDCK Epithelial CellsR01GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 1986 to 2015
$3.3M
NCI NIH HHS T32 CA009151NCI NIH HHS T32 CA09151NIGMS NIH HHS GM35527NIGMS NIH HHS R01 GM035527NIGMS NIH HHS R37 GM035527
6 · The paper itself

Abstract

Cell-cell contact formation is a dynamic process requiring the coordination of cadherin-based cell-cell adhesion and integrin-based cell migration. A genome-wide RNA interference screen for proteins required specifically for cadherin-dependent cell-cell adhesion identified an Elmo-Dock complex. This was unexpected as Elmo-Dock complexes act downstream of integrin signaling as Rac guanine-nucleotide exchange factors. In this paper, we show that Elmo2 recruits Dock1 to initial cell-cell contacts in Madin-Darby canine kidney cells. At cell-cell contacts, both Elmo2 and Dock1 are essential for the rapid recruitment and spreading of E-cadherin, actin reorganization, localized Rac and Rho GTPase activities, and the development of strong cell-cell adhesion. Upon completion of cell-cell adhesion, Elmo2 and Dock1 no longer localize to cell-cell contacts and are not required subsequently for the maintenance of cell-cell adhesion. These studies show that Elmo-Dock complexes are involved in both integrin- and cadherin-based adhesions, which may help to coordinate the transition of cells from migration to strong cell-cell adhesion.

Indexed as

Cell AdhesionActin CytoskeletonAnimalsCadherinsCytoskeletal ProteinsDogsGene Knockdown TechniquesMadin Darby Canine Kidney CellsMicroscopy, FluorescenceProtein Transportrac GTP-Binding Proteinsrho GTP-Binding ProteinsCadherinsCytoskeletal Proteinsrac GTP-Binding Proteinsrho GTP-Binding Proteins

Identifiers

PMID25452388
PMCPMC4259811
OpenAlexW2088271180

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.