Evidence map›Paper›PMID 19435801›Full record

ArticleJournal of cell science2009

A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells.

Alok Tomar, Ssang-Taek Lim, Yangmi Lim, David D Schlaepfer

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 131 citations in OpenAlex.

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  15. EphA2 signaling within integrin adhesions regulates fibrillar adhesion elongation and fibronectin deposition.Matrix biology : journal of the International Society for Matrix Biology · 2021
    Article
  16. A spatial model of YAP/TAZ signaling reveals how stiffness, dimensionality, and shape contribute to emergent outcomes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. Article
  18. Review
  19. Article
  20. p190RhoGAPs, theCells · 2019
    Review

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Alok TomarUniversity of California San Diego, Moores Cancer Center, Department of Reproductive Medicine, La Jolla, CA 92093, USA.
Ssang-Taek Lim
Yangmi Lim
David D Schlaepfer
University of California, San Diego · US

Funding

FAK Signals Controlling Endothelial Cell Survival and MotilityR01HL093156 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SCHLAEPFER, DAVID D · 2008 to 2011
$2.0M
Genetic Analysis of FAK ActivityR01GM087400 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SCHLAEPFER, DAVID D · 2009 to 2012
$1.2M
NHLBI NIH HHS HL093156NIGMS NIH HHS GM087400NIGMS NIH HHS R01 GM087400
6 · The paper itself

Abstract

Directional motility is a complex process requiring the spatiotemporal integration of signals that regulate cytoskeletal changes, and the establishment of an anteroposterior or polarized cell axis. Focal adhesion kinase (FAK) promotes cell migration, but a molecular role for FAK in promoting cell polarity remains undefined. Here, using wound healing and Golgi-reorientation analyses, we show that fibroblast, endothelial and carcinoma polarity during cell migration requires FAK and is associated with a complex between FAK, p120RasGAP and p190RhoGAP (p190A), leading to p190A tyrosine phosphorylation. Fibronectin-integrin-mediated FAK activation and phosphorylation promote SH2-mediated binding of p120RasGAP to FAK and FAK-mediated p190A tyrosine phosphorylation. The association of p120RasGAP with FAK facilitates the formation of a FAK-p120RasGAP-p190A complex targeted to leading-edge focal adhesions by FAK. Knockdown of p120RasGAP, mutation of FAK Y397 or inhibition of FAK activity prevent the association of FAK with p190A and subsequent tyrosine phosphorylation of p190A, and result in the loss of cell polarity. Because reconstitution of FAK-null fibroblasts with FAK or a Pyk2-FAK chimera restore the normal decrease in RhoA GTP binding upon cell spreading on fibronectin, our studies support a model whereby FAK activity facilitates the recruitment and stabilization of a p120RasGAP-p190A complex at leading-edge focal adhesions connected to the transient inhibition of RhoA activity and the regulation of cell polarity.

Indexed as

Cell PolarityAnimalsCarcinomaCell MovementEndothelial CellsFibroblastsFocal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesFocal AdhesionsGTPase-Activating ProteinsHumansMiceMice, KnockoutMultiprotein Complexesp120 GTPase Activating ProteinPhosphorylationArhgap35 protein, mouseFocal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGTPase-Activating ProteinsMultiprotein Complexesp120 GTPase Activating ProteinPtk2b protein, mouseRecombinant Fusion ProteinsRepressor ProteinsTyrosine

Identifiers

PMID19435801
PMCPMC2684836
OpenAlexW2164017897

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.