Evidence map›Paper›PMID 9425168›Full record

ArticleThe Journal of cell biology1998

Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration.

L A Cary, D C Han, T R Polte, S K Hanks, J L Guan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed
19.4field-weighted citation impact, top 1% 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

153 citing papers in PubMed, 497 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Squishy matters - Corneal mechanobiology in health and disease.Progress in retinal and eye research · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

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

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 2 institutions in 1 country.

L A CaryCancer Biology Laboratories, Department of Pathology, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853, USA.
D C Han
T R Polte
S K Hanks
J L Guan
Vanderbilt University · USCornell University · US

Funding

FUNCTIONAL STUDIES OF FOCAL ADHESION KINASER01GM049882 · NIGMS · VANDERBILT UNIVERSITY · PI HANKS, STEVEN K. · 1995 to 2010
$3.2M
Molecular Analysis of Signal Transduction in Cell MigrationR01GM048050 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GUAN, JUN-LIN · 1992 to 2009
$2.5M
NIGMS NIH HHS GM48050NIGMS NIH HHS GM49882NIGMS NIH HHS R01 GM048050NIGMS NIH HHS R01 GM049882
6 · The paper itself

Abstract

Previously we have demonstrated that focal adhesion kinase (FAK)-promoted migration on fibronectin (FN) by its overexpression in CHO cells is dependent on FAK autophosphorylation at Y397 and subsequent binding of Src to this site. In this report, we have examined the role of FAK association with Grb2 and p130(Cas), two downstream events of the FAK/Src complex that could mediate integrin-stimulated activation of extracellular signal-regulated kinases (Erks). We show that a Y925F FAK mutant was able to promote cell migration as efficiently as FAK and that the transfected FAK demonstrated no detectable association with Grb2 in CHO cells. In contrast, cells expressing a FAK P712/715A mutant demonstrated a level of migration comparable to that of control cells. This mutation did not affect FAK kinase activity, autophosphorylation, or Src association but did significantly reduce p130(Cas) association with FAK. Furthermore, FAK expression in CHO cells increased tyrosine phosphorylation of p130(Cas) and its subsequent binding to several SH2 domains, which depended on both the p130(Cas) binding site and the Src binding site. However, we did not detect increased activation of Erks in cells expressing FAK, and the MEK inhibitor PD98059 did not decrease FAK-promoted cell migration. Finally, we show that coexpression of p130(Cas) further increased cell migration on FN and coexpression of the p130(Cas) SH3 domain alone functioned as a dominant negative mutant and decreased cell migration. Together, these results demonstrate that p130(Cas), but not Grb2, is a mediator of FAK-promoted cell migration and suggest that FAK/ p130(Cas) complex targets downstream pathways other than Erks in mediating FAK-promoted cell migration.

Indexed as

ProteinsAnimalsBinding SitesCell Adhesion MoleculesChemotaxisCHO CellsCricetinaeCrk-Associated Substrate ProteinFocal Adhesion Protein-Tyrosine KinasesGlutathione TransferaseMutagenesis, Site-DirectedPhosphoproteinsPoint MutationPolymerase Chain ReactionProtein-Tyrosine KinasesRecombinant Fusion ProteinsCell Adhesion MoleculesCrk-Associated Substrate ProteinFocal Adhesion Protein-Tyrosine KinasesGlutathione TransferasePhosphoproteinsProteinsProtein-Tyrosine KinasesRecombinant Fusion ProteinsRetinoblastoma-Like Protein p130

Identifiers

PMID9425168
PMCPMC2132604
OpenAlexW2034246730

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.