Evidence map›Paper›PMID 21937717›Full record

ArticleMolecular biology of the cell2011

β3 integrin-EGF receptor cross-talk activates p190RhoGAP in mouse mammary gland epithelial cells.

Nikolas Balanis, Masaaki Yoshigi, Michael K Wendt, William P Schiemann, Cathleen R Carlin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  8. Integrins and Cell Metabolism: An Intimate Relationship Impacting Cancer.International journal of molecular sciences · 2017
    Review
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  12. Review
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  17. Cellular functions regulated by phosphorylation of EGFR on Tyr845.International journal of molecular sciences · 2013
    Review
  18. 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

5 authors at 3 institutions in 1 country.

Nikolas BalanisDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106, USA.
Masaaki Yoshigi
Michael K Wendt
William P Schiemann
Cathleen R Carlin
Case Western Reserve University · USCase Comprehensive Cancer CenterUniversity of Utah · US

Funding

TUMOR METABOLISM PROGRAMP30CA043703 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MARK R CHANCE · 1987 to 2026
$142.3M
CLEVELAND TRAINING PROGRAM IN CARDIOVASCULAR RESEARCHT32HL007653 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI DUBYAK, GEORGE R · 1988 to 2008
$3.5M
Integrin-Mediated Regulation of TGF-Beta Signaling and TumorigenesisR01CA129359 · NCI · UNIVERSITY OF COLORADO DENVER · PI SCHIEMANN, WILLIAM · 2007 to 2016
$2.9M
Modulation of Rab7-Dependent Degradative Pathways by Novel Adenovirus ProteinR01GM081498 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI CARLIN, CATHLEEN R · 2009 to 2012
$1.3M
NCI NIH HHS CA129359NCI NIH HHS P30 CA043703NCI NIH HHS R01 CA129359NHLBI NIH HHS HL007653NHLBI NIH HHS T32 HL007653NIGMS NIH HHS GM081498NIGMS NIH HHS R01 GM081498
6 · The paper itself

Abstract

Active RhoA localizes to plasma membrane, where it stimulates formation of focal adhesions and stress fibers. RhoA activity is inhibited by p190RhoGAP following integrin-mediated cell attachment to allow sampling of new adhesive environments. p190RhoGAP is itself activated by Src-dependent tyrosine phosphorylation, which facilitates complex formation with p120RasGAP. This complex then translocates to the cell surface, where p190RhoGAP down-regulates RhoA. Here we demonstrate that the epidermal growth factor receptor (EGFR) cooperates with β3 integrin to regulate p190RhoGAP activity in mouse mammary gland epithelial cells. Adhesion to fibronectin stimulates tyrosine phosphorylation of the EGFR in the absence of receptor ligands. Use of a dominant inhibitory EGFR mutant demonstrates that fibronectin-activated EGFR recruits p120RasGAP to the cell periphery. Expression of an inactive β3 integrin subunit abolishes p190RhoGAP tyrosine phosphorylation, demonstrating a mechanistic link between β3 integrin-activated Src and EGFR regulation of the RhoA inhibitor. The β3 integrin/EGFR pathway also has a positive role in formation of filopodia. Together our data suggest that EGFR constitutes an important intrinsic migratory cue since fibronectin is a key component of the microenvironment in normal mammary gland development and breast cancer. Our data also suggest that EGFR expressed at high levels has a role in eliciting cell shape changes associated with epithelial-to-mesenchymal transition.

Indexed as

Receptor Cross-TalkAnimalsCell AdhesionCell LineCell MembraneCell MovementEpidermal Growth FactorEpithelial CellsEpithelial-Mesenchymal TransitionErbB ReceptorsFibronectinsFocal AdhesionsGTPase-Activating ProteinsIntegrin beta3Mammary Glands, AnimalMiceArhgap5 protein, mouseEpidermal Growth FactorErbB ReceptorsFibronectinsGTPase-Activating ProteinsIntegrin beta3p120 GTPase Activating ProteinrhoA GTP-Binding ProteinTyrosine

Identifiers

PMID21937717
PMCPMC3216655
OpenAlexW2082999328

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.