Evidence map›Paper›PMID 25307943›Full record

ArticleProtein science : a publication of the Protein Society2015

Actin-induced dimerization of palladin promotes actin-bundling.

Ravi Vattepu, Rahul Yadav, Moriah R Beck

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

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  6. Functional comparison of full-length palladin to isolated actin binding domain.Protein science : a publication of the Protein Society · 2023
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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

3 authors at 1 institution in 1 country.

Ravi VattepuChemistry Department, Wichita State University, Wichita, Kansas, 67260.
Rahul Yadav
Moriah R Beck
Wichita State University · US

Funding

Mentoring CoreP20GM103418 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI SUSAN J. BROWN · 2012 to 2026
$63.0M
TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI HOLYOAK, TODD · 2002 to 2011
$20.1M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
NCRR NIH HHS 5P20RR017708NIGMS NIH HHS 8P20GM103420NIGMS NIH HHS P20GM103418NIGMS NIH HHS P20 GM103420
6 · The paper itself

Abstract

A subset of actin binding proteins is able to form crosslinks between two or more actin filaments, thus producing structures of parallel or networked bundles. These actin crosslinking proteins interact with actin through either bivalent binding or dimerization. We recently identified two binding sites within the actin binding domain of palladin, an actin crosslinking protein that plays an important role in normal cell adhesion and motility during wound healing and embryonic development. In this study, we show that actin induces dimerization of palladin. Furthermore, the extent of dimerization reflects earlier comparisons of actin binding and bundling between different domains of palladin. On the basis of these results we hypothesized that actin binding may promote a conformational change that results in dimerization of palladin, which in turn may drive the crosslinking of actin filaments. The proximal distance between two actin binding sites on crosslinking proteins determines the ultrastructural properties of the filament network, therefore we also explored interdomain interactions using a combination of chemical crosslinking experiments and actin cosedimentation assays. Limited proteolysis data reveals that palladin is less susceptible to enzyme digestion after actin binding. Our results suggest that domain movements in palladin are necessary for interactions with actin and are induced by interactions with actin filaments. Accordingly, we put forth a model linking the structural changes to functional dynamics.

Indexed as

Actin CytoskeletonActinsMicrofilament ProteinsPhosphoproteinsProtein BindingProtein ConformationProtein MultimerizationProtein Structure, TertiaryProteolysisRecombinant ProteinsActinsMicrofilament ProteinsPhosphoproteinsRecombinant Proteinsactinbundlingcrosslinkingdimerizationpalladin

Identifiers

PMID25307943
PMCPMC4282413
OpenAlexW1585804001

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.