Evidence map›Paper›PMID 17652459›Full record

ArticleMolecular biology of the cell2007

The Abl-related gene tyrosine kinase acts through p190RhoGAP to inhibit actomyosin contractility and regulate focal adhesion dynamics upon adhesion to fibronectin.

Justin G Peacock, Ann L Miller, William D Bradley, Olga C Rodriguez, Donna J Webb, Anthony J Koleske

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 85 citations in OpenAlex.

  1. Frontiers in cell and developmental biology · 2025
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  6. Abl2:Cortactin Interactions Regulate Dendritic Spine Stability via Control of a Stable Filamentous Actin Pool.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
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  8. 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

6 authors at 4 institutions in 3 countries.

Justin G PeacockDepartment of Molecular Biophysics and Biochemistry, Department of Neurobiology, and Interdepartmental Neuroscience Program, Yale University, New Haven, CT 06511, USA.
Ann L Miller
William D Bradley
Olga C Rodriguez
Donna J Webb
Anthony J Koleske
Institute of Molecular Biology and Biophysics · RUScripps Research Institute · USVanderbilt University · USYale University · US

Funding

Roles of Abl and Arg Neuronal DevelopmentR01NS039475 · NINDS · YALE UNIVERSITY · PI KOLESKE, ANTHONY J · 2000 to 2012
$4.3M
Supplement to Regulation of invadopodia formation in breast cancer cellsR01CA133346 · NCI · YALE UNIVERSITY · PI KOLESKE, ANTHONY J · 2009 to 2016
$2.3M
Biochemical screen--regulators of neuronal morphogenesisR21MH077306 · NIMH · YALE UNIVERSITY · PI KOLESKE, ANTHONY J · 2006 to 2007
$398k
Regulation of cell motility by Arg tyrosine kinaseF31NS045477 · NINDS · YALE UNIVERSITY · PI MILLER, ANN LOUISE · 2003 to 2004
$78k
NCI NIH HHS R01 CA133346NIMH NIH HHS MH77306NIMH NIH HHS R21 MH077306NINDS NIH HHS F31 NS045477NINDS NIH HHS NS39754NINDS NIH HHS NS45477NINDS NIH HHS R01 NS039475
6 · The paper itself

Abstract

In migrating cells, actin polymerization promotes protrusion of the leading edge, whereas actomyosin contractility powers net cell body translocation. Although they promote F-actin-dependent protrusions of the cell periphery upon adhesion to fibronectin (FN), Abl family kinases inhibit cell migration on FN. We provide evidence here that the Abl-related gene (Arg/Abl2) kinase inhibits fibroblast migration by attenuating actomyosin contractility and regulating focal adhesion dynamics. arg-/- fibroblasts migrate at faster average speeds than wild-type (wt) cells, whereas Arg re-expression in these cells slows migration. Surprisingly, the faster migrating arg-/- fibroblasts have more prominent F-actin stress fibers and focal adhesions and exhibit increased actomyosin contractility relative to wt cells. Interestingly, Arg requires distinct functional domains to inhibit focal adhesions and actomyosin contractility. The kinase domain-containing Arg N-terminal half can act through the RhoA inhibitor p190RhoGAP to attenuate stress fiber formation and cell contractility. However, Arg requires both its kinase activity and its cytoskeleton-binding C-terminal half to fully inhibit focal adhesions. Although focal adhesions do not turn over efficiently in the trailing edge of arg-/- cells, the increased contractility of arg-/- cells tears the adhesions from the substrate, allowing for the faster migration observed in these cells. Together, our data strongly suggest that Arg inhibits cell migration by restricting actomyosin contractility and regulating its coupling to the substrate through focal adhesions.

Indexed as

ActomyosinAnimalsCell AdhesionCell MovementDNA-Binding ProteinsFibroblastsFibronectinsFocal AdhesionsGTPase-Activating ProteinsMiceMutant ProteinsProtein Structure, TertiaryProtein-Tyrosine KinasesRepressor Proteinsrho GTP-Binding ProteinsStress FibersActomyosinARG tyrosine kinaseArhgap35 protein, mouseDNA-Binding ProteinsFibronectinsGTPase-Activating ProteinsMutant ProteinsProtein-Tyrosine KinasesRepressor Proteinsrho GTP-Binding Proteins

Identifiers

PMID17652459
PMCPMC1995720
OpenAlexW2127611865

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.