Evidence map›Paper›PMID 26607837›Full record

ArticleThe Biochemical journal2016

Actin polymerization is stimulated by actin cross-linking protein palladin.

Ritu Gurung, Rahul Yadav, Joseph G Brungardt, Albina Orlova, Edward H Egelman, Moriah R Beck

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-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

19 citing papers in PubMed, 33 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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  14. The Role of Palladin in Podocytes.Journal of the American Society of Nephrology : JASN · 2018
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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

6 authors at 2 institutions in 1 country.

Ritu GurungChemistry Department, Wichita State University, Wichita, KS 67260, U.S.A.
Rahul YadavChemistry Department, Wichita State University, Wichita, KS 67260, U.S.A.
Joseph G BrungardtChemistry Department, Wichita State University, Wichita, KS 67260, U.S.A.
Albina OrlovaDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908, U.S.A.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908, U.S.A.
Moriah R BeckChemistry Department, Wichita State University, Wichita, KS 67260, U.S.A. moriah.beck@wichita.edu.
Wichita State University · USUniversity of Virginia · 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 Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
Probing Actin Filament Assembly, Structure, and Dynamics by PalladinR15GM120670 · NIGMS · WICHITA STATE UNIVERSITY · PI BECK, MORIAH R · 2016 to 2016
$415k
NCRR NIH HHS 5P20RR017708NCRR NIH HHS P20 RR017708NIGMS NIH HHS 8P20GM103420NIGMS NIH HHS P20 GM103418NIGMS NIH HHS P20GM103418NIGMS NIH HHS P20 GM103420NIGMS NIH HHS P30 GM110761NIGMS NIH HHS R01 GM081303NIGMS NIH HHS R15 GM120670Wellcome Trust
6 · The paper itself

Abstract

The actin scaffold protein palladin regulates both normal cell migration and invasive cell motility, processes that require the co-ordinated regulation of actin dynamics. However, the potential effect of palladin on actin dynamics has remained elusive. In the present study, we show that the actin-binding immunoglobulin-like domain of palladin, which is directly responsible for both actin binding and bundling, also stimulates actin polymerization in vitro. Palladin eliminated the lag phase that is characteristic of the slow nucleation step of actin polymerization. Furthermore, palladin dramatically reduced depolymerization, slightly enhanced the elongation rate, and did not alter the critical concentration. Microscopy and in vitro cross-linking assays reveal differences in actin bundle architecture when palladin is incubated with actin before or after polymerization. These results suggest a model whereby palladin stimulates a polymerization-competent form of globular or monomeric actin (G-actin), akin to metal ions, either through charge neutralization or through conformational changes.

Indexed as

ActinsAnimalsCytoskeletal ProteinsPolymerizationRabbitsStatic ElectricityActinsCytoskeletal Proteinsactincross-linkingkineticsnucleationpolymerization

Identifiers

PMID26607837
PMCPMC4912051
OpenAlexW2260822634

What OpenQuestion holds

Textmetadata
LicenceTDM
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.