Evidence map›Paper›PMID 20430882›Full record

ArticleThe Journal of biological chemistry2010

Dynamics and mechanism of p130Cas localization to focal adhesions.

Dominique M Donato, Larisa M Ryzhova, Leslie M Meenderink, Irina Kaverina, Steven K Hanks

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 66 citations in OpenAlex.

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  16. Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017
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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

5 authors at 1 institution in 1 country.

Dominique M DonatoDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Larisa M Ryzhova
Leslie M Meenderink
Irina Kaverina
Steven K Hanks
Vanderbilt University · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007347 · NIGMS · VANDERBILT UNIVERSITY · PI WILLIAMS, CHRISTOPHER S. · 1985 to 2023
$26.3M
MULTIDISCIPLINARY BASIC RESEARCH TRAINING IN CANCERT32CA009592 · NCI · VANDERBILT UNIVERSITY · PI Justin M Balko, Julie A Rhoades (Sterling) · 1987 to 2026
$10.4M
FUNCTIONAL STUDIES OF FOCAL ADHESION KINASER01GM049882 · NIGMS · VANDERBILT UNIVERSITY · PI HANKS, STEVEN K. · 1995 to 2010
$3.2M
Spatial Regulation of Cytoskeletal AsymmetryR01GM078373 · NIGMS · VANDERBILT UNIVERSITY · PI KAVERINA, IRINA · 2008 to 2017
$3.2M
NCI NIH HHS T32 CA009592NCI NIH HHS T32-CA09592NIDDK NIH HHS P30 DK058404NIDDK NIH HHS P30-DK058404NIGMS NIH HHS R01 GM049882NIGMS NIH HHS R01-GM049882NIGMS NIH HHS R01 GM078373NIGMS NIH HHS R01-GM78373NIGMS NIH HHS T32 GM007347NIGMS NIH HHS T32-GM07347
6 · The paper itself

Abstract

The docking protein p130Cas is a major Src substrate involved in integrin signaling and mechanotransduction. Tyrosine phosphorylation of p130Cas in focal adhesions (FAs) has been linked to enhanced cell migration, invasion, proliferation, and survival. However, the mechanism of p130Cas targeting to FAs is uncertain, and dynamic aspects of its localization have not been explored. Using live cell microscopy, we show that fluorophore-tagged p130Cas is a component of FAs throughout the FA assembly and disassembly stages, although it resides transiently in FAs with a high mobile fraction. Deletion of either the N-terminal Src homology 3 (SH3) domain or the Cas-family C-terminal homology (CCH) domain significantly impaired p130Cas FA localization, and deletion of both domains resulted in full exclusion. Focal adhesion kinase was implicated in the FA targeting function of the p130Cas SH3 domain. Consistent with their roles in FA targeting, both the SH3 and CCH domains were found necessary for p130Cas to fully undergo tyrosine phosphorylation and promote cell migration. By revealing the capacity of p130Cas to function in FAs throughout their lifetime, clarifying FA targeting mechanism, and demonstrating the functional importance of the highly conserved CCH domain, our results advance the understanding of an important aspect of integrin signaling.

Indexed as

AnimalsAntibodies, MonoclonalCell MovementCrk-Associated Substrate ProteinFibroblastsFocal AdhesionsGenes, ReporterGenetic VariationImmunoblottingLuminescent ProteinsMicePaxillinPhosphorylationPlasmidsPolymerase Chain Reactionsrc-Family KinasesAntibodies, MonoclonalCrk-Associated Substrate ProteinLuminescent ProteinsPaxillinsrc-Family Kinases

Identifiers

PMID20430882
PMCPMC2898362
OpenAlexW2028116568

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.