Evidence map›Paper›PMID 12482962›Full record

ArticleMolecular and cellular biology2003

Targeted disruption of the murine zyxin gene.

Laura M Hoffman, David A Nix, Beverly Benson, Ray Boot-Hanford, Erika Gustafsson, Colin Jamora, A Sheila Menzies, Keow Lin Goh, Christopher C Jensen, Frank B Gertler and 3 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

53 citing papers in PubMed, 98 citations in OpenAlex.

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  12. TRIP6 functions in brain ciliogenesis.Nature communications · 2021
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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

13 authors at 6 institutions in 2 countries.

Laura M HoffmanHuntsman Cancer Institute and Department of Biology, University of Utah, Salt Lake City 84112, USA.
David A Nix
Beverly Benson
Ray Boot-Hanford
Erika Gustafsson
Colin Jamora
A Sheila Menzies
Keow Lin Goh
Christopher C Jensen
Frank B Gertler
Elaine Fuchs
Reinhard Fässler
Mary C Beckerle
Huntsman Cancer Institute · USLund University · SEMassachusetts Institute of Technology · USUniversity of Utah · USHoward Hughes Medical Institute · USUniversity of Chicago · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Jared P Rutter · 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
CELLULAR AND DEVELOPMENTAL FUNCTIONS OF MENAR01GM058801 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GERTLER, FRANK B · 1999 to 2012
$3.8M
MULTIDISCPLINARY BASIC CANCER RESEARCH TRAININGT32CA009602 · NCI · UNIVERSITY OF UTAH · PI LEMONS, RICHARD S · 1988 to 1998
–
NCI NIH HHS P30 CA042014NCI NIH HHS T32 CA009602NCI NIH HHS T32-CA09602NIGMS NIH HHS GM50877NIGMS NIH HHS GM58801NIGMS NIH HHS R01 GM050877NIGMS NIH HHS R01 GM058801
6 · The paper itself

Abstract

Zyxin is an evolutionarily conserved protein that is concentrated at sites of cell adhesion, where it associates with members of the Enabled (Ena)/vasodilator-stimulated phosphoprotein (VASP) family of cytoskeletal regulators and is postulated to play a role in cytoskeletal dynamics and signaling. Zyxin transcripts are detected throughout murine embryonic development, and the protein is widely expressed in adults. Here we used a reverse genetic approach to examine the consequences of loss of zyxin function in the mouse. Mice that lack zyxin function are viable and fertile and display no obvious histological abnormalities in any of the organs examined. Because zyxin contributes to the localization of Ena/VASP family members at certain subcellular locations, we carefully examined the zyxin(-/-) mice for evidence of defects that have been observed when Ena/VASP proteins are compromised in the mouse. Specifically, we evaluated blood platelet function, nervous system development, and skin architecture but did not detect any defects in these systems. Zyxin is the founding member of a family of proteins that also includes the lipoma preferred partner (LPP) and thyroid receptor-interacting protein 6 (TRIP6). These zyxin family members display patterns of expression that significantly overlap that of zyxin. Western blot analysis indicates that there is no detectable upregulation of either LPP or TRIP6 expression in tissues derived from zyxin-null mice. Because zyxin family members may have overlapping functions, a comprehensive understanding of the role of these proteins in the mouse will require the generation of compound mutations in which multiple zyxin family members are simultaneously compromised.

Indexed as

Adaptor Proteins, Signal TransducingGene Expression Regulation, DevelopmentalAmino Acid SequenceAnimalsATPases Associated with Diverse Cellular ActivitiesBlood PlateletsBrainCarrier ProteinsCell Adhesion MoleculesCytoskeletal ProteinsEpidermisFertilityLIM Domain ProteinsLungMetalloproteinsMiceAdaptor Proteins, Signal TransducingATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell Adhesion MoleculesCytoskeletal ProteinsEnah protein, mouseLIM Domain ProteinsLpp protein, mouseMetalloproteinsMicrofilament ProteinsPhosphoproteinsProteasome Endopeptidase ComplexPSMC5 protein, humanTranscription FactorsVasodilator-Stimulated PhosphoproteinZyxinZyx protein, mouse

Identifiers

PMID12482962
PMCPMC140673
OpenAlexW2138498894

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.