Evidence map›Paper›PMID 23788645›Full record

ArticleThe Journal of biological chemistry2013

Danio rerio αE-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αE-catenin.

Phillip W Miller, Sabine Pokutta, Agnidipta Ghosh, Steven C Almo, William I Weis, W James Nelson, Adam V Kwiatkowski

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  12. Measuring Protein Binding to F-actin by Co-sedimentation.Journal of visualized experiments : JoVE · 2017
    Article
  13. Structural and functional characterization ofThe Journal of biological chemistry · 2017
    Article
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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

7 authors at 2 institutions in 1 country.

Phillip W MillerDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305, USA.
Sabine Pokutta
Agnidipta Ghosh
Steven C Almo
William I Weis
W James Nelson
Adam V Kwiatkowski
Stanford University · USAlbert Einstein College of Medicine · US

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
Topogenesis of NA/K-ATPASE in Polarized Epithelial CellsR37GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 2003 to 2012
$7.4M
Assemby , dynamics and evolution of cell-cell and cell-matrix adhesionsU01GM094663 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI GINSBERG, MARK HOWARD · 2010 to 2014
$6.4M
Topogenesis of Na/K-ATPase in Polarized MDCK Epithelial CellsR01GM035527 · NIGMS · STANFORD UNIVERSITY · PI NELSON, W. JAMES · 1986 to 2015
$3.3M
NIGMS NIH HHS GM007276NIGMS NIH HHS GM35527NIGMS NIH HHS R01 GM035527NIGMS NIH HHS R37 GM035527NIGMS NIH HHS T32 GM007276NIGMS NIH HHS U01 GM094663NIGMS NIH HHS U01 GM94663
6 · The paper itself

Abstract

It is unknown whether homologs of the cadherin·catenin complex have conserved structures and functions across the Metazoa. Mammalian αE-catenin is an allosterically regulated actin-binding protein that binds the cadherin·β-catenin complex as a monomer and whose dimerization potentiates F-actin association. We tested whether these functional properties are conserved in another vertebrate, the zebrafish Danio rerio. Here we show, despite 90% sequence identity, that Danio rerio and Mus musculus αE-catenin have striking functional differences. We demonstrate that D. rerio αE-catenin is monomeric by size exclusion chromatography, native PAGE, and small angle x-ray scattering. D. rerio αE-catenin binds F-actin in cosedimentation assays as a monomer and as an α/β-catenin heterodimer complex. D. rerio αE-catenin also bundles F-actin, as shown by negative stained transmission electron microscopy, and does not inhibit Arp2/3 complex-mediated actin nucleation in bulk polymerization assays. Thus, core properties of α-catenin function, F-actin and β-catenin binding, are conserved between mouse and zebrafish. We speculate that unique regulatory properties have evolved to match specific developmental requirements.

Indexed as

alpha CateninAnimalsCarrier ProteinsChromatography, GelMiceMicrofilament ProteinsNative Polyacrylamide Gel ElectrophoresisProtein BindingScattering, RadiationZebrafishalpha CateninCarrier ProteinsF-actin-binding proteinsMicrofilament ProteinsActinAdherens JunctionCateninCell AdhesionProtein Evolution

Identifiers

PMID23788645
PMCPMC3829323
OpenAlexW2026309041

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.