Evidence map›Paper›PMID 37298410›Full record

ArticleInternational journal of molecular sciences2023

Plakophilin-3 Binds the Membrane and Filamentous Actin without Bundling F-Actin.

Jyoti Gupta, Erumbi S Rangarajan, Regina B Troyanovsky, Indrajyoti Indra, Sergey M Troyanovsky, Tina Izard

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
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.

Jyoti GuptaCell Adhesion Laboratory, UF Scripps, Jupiter, FL 33458, USA.
Erumbi S RangarajanCell Adhesion Laboratory, UF Scripps, Jupiter, FL 33458, USA.
Regina B TroyanovskyDepartment of Dermatology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 606112, USA.
Indrajyoti IndraDepartment of Dermatology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 606112, USA.
Sergey M TroyanovskyDepartment of Dermatology, The Feinberg School of Medicine, Northwestern University, Chicago, IL 606112, USA.ORCID 0000-0001-7368-9708
Tina IzardCell Adhesion Laboratory, UF Scripps, Jupiter, FL 33458, USA.
Northwestern University · USScripps Research Institute · US

Funding

Cadherin Clusters and actin filamentsR01AR070166 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Sergey M Troyanovsky · 2016 to 2026
$4.1M
Molecular Mechanisms of Cell AdhesionR35GM139604 · NIGMS · UNIVERSITY OF FLORIDA · PI TINA IZARD · 2021 to 2026
$2.8M
Intercellular junctions and cell polarityR01GM148571 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Sergey M Troyanovsky · 2023 to 2026
$1.8M
NIAMS NIH HHS R01 AR070166NIGMS NIH HHS R01 GM148571NIGMS NIH HHS R35 GM139604
6 · The paper itself

Abstract

Plakophilin-3 is a ubiquitously expressed protein found widely in epithelial cells and is a critical component of desmosomes. The plakophilin-3 carboxy-terminal domain harbors nine armadillo repeat motifs with largely unknown functions. Here, we report the 5 Å cryogenic electron microscopy (cryoEM) structure of the armadillo repeat motif domain of plakophilin-3, one of the smaller cryoEM structures reported to date. We find that this domain is a monomer or homodimer in solution. In addition, using an in vitro actin co-sedimentation assay, we show that the armadillo repeat domain of plakophilin-3 directly interacts with F-actin. This feature, through direct interactions with actin filaments, could be responsible for the observed association of extra-desmosomal plakophilin-3 with the actin cytoskeleton directly attached to the adherens junctions in A431 epithelial cells. Further, we demonstrate, through lipid binding analyses, that plakophilin-3 can effectively be recruited to the plasma membrane through phosphatidylinositol-4,5-bisphosphate-mediated interactions. Collectively, we report on novel properties of plakophilin-3, which may be conserved throughout the plakophilin protein family and may be behind the roles of these proteins in cell-cell adhesion.

Indexed as

ActinsPlakophilinsActin CytoskeletonDesmosomesActinsPlakophilinsactin cytoskeletonarmadillodesmosomesphosphatidylinositol 4,5-bisphosphateplakophilinplasma membrane

Identifiers

PMID37298410
PMCPMC10253835
OpenAlexW4380224985

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.