Evidence map›Paper›PMID 10373530›Full record

ArticleMolecular and cellular biology1999

Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2.

J D Owen, P J Ruest, D W Fry, S K Hanks

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
7.8field-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

137 citing papers in PubMed, 395 citations in OpenAlex.

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77 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

4 authors at 1 institution in 1 country.

J D OwenDepartment of Cell Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
P J Ruest
D W Fry
S K Hanks
Vanderbilt University · US

Funding

FUNCTIONAL STUDIES OF FOCAL ADHESION KINASER01GM049882 · NIGMS · VANDERBILT UNIVERSITY · PI HANKS, STEVEN K. · 1995 to 2010
$3.2M
TRAINING PROGRAM IN BREAST CANCER RESEARCHT32CA078136 · NCI · VANDERBILT UNIVERSITY · PI ARTEAGA, CARLOS L · 1998 to 2007
$2.4M
ALPHA CHEMOKINES AND ALCOHOLIC LIVER DISEASEF31AA005408 · NIAAA · VANDERBILT UNIVERSITY · PI OWEN, JAMES D · 1995 to 1997
–
NCI NIH HHS T32 CA078136NCI NIH HHS T32-CA78136NIAAA NIH HHS F31 AA005408NIAAA NIH HHS F31-AA05408NIGMS NIH HHS R01 GM049882NIGMS NIH HHS R01-GM49882
6 · The paper itself

Abstract

Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase involved in integrin-mediated control of cell behavior. Following cell adhesion to components of the extracellular matrix, FAK becomes phosphorylated at multiple sites, including tyrosines 397, 576, and 577. Tyr-397 is an autophosphorylation site that promotes interaction with c-Src or Fyn. Tyr-576 and Tyr-577 lie in the putative activation loop of the kinase domain, and FAK catalytic activity may be elevated through phosphorylation of these residues by associated Src family kinase. Recent studies have implicated FAK as a positive regulator of cell spreading and migration. To further study the mechanism of adhesion-induced FAK activation and the possible role and signaling requirements for FAK in cell spreading and migration, we utilized the tetracycline repression system to achieve inducible expression of either wild-type FAK or phosphorylation site mutants in fibroblasts derived from FAK-null mouse embryos. Using these Tet-FAK cells, we demonstrated that both the FAK autophosphorylation and activation loop sites are critical for maximum adhesion-induced FAK activation and FAK-enhanced cell spreading and migration responses. Negative effects on cell spreading and migration, as well as decreased phosphorylation of the substrate p130(Cas), were observed upon induced expression of the FAK autophosphorylation site mutant. These negative effects appear to result from an inhibition of integrin-mediated signaling by the FAK-related kinase Pyk2/CAKbeta/RAFTK/CadTK.

Indexed as

Proteins3T3 CellsAnimalsBinding SitesCatalysisCell AdhesionCell Adhesion MoleculesCell MovementCrk-Associated Substrate ProteinFibronectinsFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesGene ExpressionMicePhosphoproteinsBcar1 protein, mouseCell Adhesion MoleculesCrk-Associated Substrate ProteinFibronectinsFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesPhosphoproteinsProteinsProtein-Tyrosine KinasesPtk2b protein, mousePtk2 protein, mouseRetinoblastoma-Like Protein p130TetracyclineTyrosine

Identifiers

PMID10373530
PMCPMC84279
OpenAlexW1845277443

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.