Evidence map›Paper›PMID 16505170›Full record

ArticleThe Journal of cell biology2006

Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling.

Laura M Hoffman, Christopher C Jensen, Susanne Kloeker, C-L Albert Wang, Masaaki Yoshigi, Mary C Beckerle

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.

0numbers the graph read from it
0cells of the map it votes in
102citing papers in PubMed
4.1field-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

102 citing papers in PubMed, 163 citations in OpenAlex.

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42 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

6 authors at 3 institutions in 1 country.

Laura M HoffmanThe Huntsman Cancer Institute and the Department of Biology,University of Utah, Salt Lake City, UT 84112, USA.
Christopher C Jensen
Susanne Kloeker
C-L Albert Wang
Masaaki Yoshigi
Mary C Beckerle
Huntsman Cancer Institute · USBoston Biomedical Research Institute · USUniversity of Utah · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI KATHARINE S ULLMAN · 1986 to 2026
$72.6M
Structure and function of stress fibers and cell adhesion sitesR01GM050877 · NIGMS · UNIVERSITY OF UTAH · PI BECKERLE, MARY C. · 1994 to 2020
$7.8M
NCI NIH HHS P30 CA042014NCI NIH HHS P30 CA42014NIGMS NIH HHS R01 GM050877NIGMS NIH HHS R01GM50877
6 · The paper itself

Abstract

Focal adhesions are specialized regions of the cell surface where integrin receptors and associated proteins link the extracellular matrix to the actin cytoskeleton. To define the cellular role of the focal adhesion protein zyxin, we characterized the phenotype of fibroblasts in which the zyxin gene was deleted by homologous recombination. Zyxin-null fibroblasts display enhanced integrin-dependent adhesion and are more migratory than wild-type fibroblasts, displaying reduced dependence on extracellular matrix cues. We identified differences in the profiles of 75- and 80-kD tyrosine-phosphorylated proteins in the zyxin-null cells. Tandem array mass spectrometry identified both modified proteins as isoforms of the actomyosin regulator caldesmon, a protein known to influence contractility, stress fiber formation, and motility. Zyxin-null fibroblasts also show deficits in actin stress fiber remodeling and exhibit changes in the molecular composition of focal adhesions, most notably by severely reduced accumulation of Ena/VASP proteins. We postulate that zyxin cooperates with Ena/VASP proteins and caldesmon to influence integrin-dependent cell motility and actin stress fiber remodeling.

Indexed as

ActinsAnimalsCalmodulin-Binding ProteinsCell AdhesionCell Adhesion MoleculesCell Line, TransformedCell MovementCells, CulturedCytoskeletal ProteinsDepsipeptidesExtracellular MatrixFibroblastsIntegrinsMetalloproteinsMiceMice, Inbred C57BLActinsCalmodulin-Binding ProteinsCell Adhesion MoleculesCytoskeletal ProteinsDepsipeptidesEnah protein, mouseIntegrinsjasplakinolideMetalloproteinsMicrofilament ProteinsPhosphoproteinsVasodilator-Stimulated PhosphoproteinZyxinZyx protein, mouse

Identifiers

PMID16505170
PMCPMC2063708
OpenAlexW2108162507

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.