Evidence map›Paper›PMID 26217016›Full record

ArticleMolecular and cellular biology2015

CRB3A Controls the Morphology and Cohesion of Cancer Cells through Ehm2/p114RhoGEF-Dependent Signaling.

Elise Loie, Lucie E Charrier, Kévin Sollier, Jean-Yves Masson, Patrick Laprise

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 55 citations in OpenAlex.

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  14. The Crumbs3 Polarity Protein.Cold Spring Harbor perspectives in biology · 2018
    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

5 authors at 1 institution in 1 country.

Elise LoieDepartment of Molecular Biology, Medical Biochemistry and Pathology/Cancer Research Center, Laval University, and CRCHU de Québec, Oncology Axis, Québec, Canada.
Lucie E CharrierDepartment of Molecular Biology, Medical Biochemistry and Pathology/Cancer Research Center, Laval University, and CRCHU de Québec, Oncology Axis, Québec, Canada.
Kévin SollierDepartment of Molecular Biology, Medical Biochemistry and Pathology/Cancer Research Center, Laval University, and CRCHU de Québec, Oncology Axis, Québec, Canada.
Jean-Yves MassonDepartment of Molecular Biology, Medical Biochemistry and Pathology/Cancer Research Center, Laval University, and CRCHU de Québec, Oncology Axis, Québec, Canada.
Patrick LapriseDepartment of Molecular Biology, Medical Biochemistry and Pathology/Cancer Research Center, Laval University, and CRCHU de Québec, Oncology Axis, Québec, Canada Patrick.Laprise@crchudequebec.ulaval.ca.
Université Laval · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmembrane protein CRB3A controls epithelial cell polarization. Elucidating the molecular mechanisms of CRB3A function is essential as this protein prevents the epithelial-to-mesenchymal transition (EMT), which contributes to tumor progression. To investigate the functional impact of altered CRB3A expression in cancer cells, we expressed CRB3A in HeLa cells, which are devoid of endogenous CRB3A. While control HeLa cells display a patchy F-actin distribution, CRB3A-expressing cells form a circumferential actomyosin belt. This reorganization of the cytoskeleton is accompanied by a transition from an ameboid cell shape to an epithelial-cell-like morphology. In addition, CRB3A increases the cohesion of HeLa cells. To perform these functions, CRB3A recruits p114RhoGEF and its activator Ehm2 to the cell periphery using both functional motifs of its cytoplasmic tail and increases RhoA activation levels. ROCK1 and ROCK2 (ROCK1/2), which are critical effectors of RhoA, are also essential to modulate the cytoskeleton and cell shape downstream of CRB3A. Overall, our study highlights novel roles for CRB3A and deciphers the signaling pathway conferring to CRB3A the ability to fulfill these functions. Thereby, our data will facilitate further investigation of CRB3A functions and increase our understanding of the cellular defects associated with the loss of CRB3A expression in cancer cells.

Indexed as

Actin CytoskeletonAnimalsCaco-2 CellsCell AdhesionCell ShapeCytoskeletal ProteinsDogsHEK293 CellsHeLa CellsHumansMadin Darby Canine Kidney CellsMembrane GlycoproteinsMyosin Type IIProtein TransportRho Guanine Nucleotide Exchange FactorsSignal TransductionARHGEF18 protein, humanCRB3 protein, humanCytoskeletal ProteinsEPB41L4B protein, humanMembrane GlycoproteinsMyosin Type IIRho Guanine Nucleotide Exchange Factors

Identifiers

PMID26217016
PMCPMC4561736
OpenAlexW2168855047

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.