Evidence map›Paper›PMID 25431851›Full record

ArticleThe Journal of investigative dermatology2015

Alpha actinin-1 regulates cell-matrix adhesion organization in keratinocytes: consequences for skin cell motility.

Kevin J Hamill, Sho Hiroyasu, Zachary T Colburn, Rosa V Ventrella, Susan B Hopkinson, Omar Skalli, Jonathan C R Jones

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of investigative dermatology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. From inflammation to remodelling: A novel BASP1Journal of advanced research · 2025
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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 4 institutions in 2 countries.

Kevin J HamillDepartment of Eye and Vision Science, Institute of Ageing and Chronic Diseases, University of Liverpool, Liverpool, UK.
Sho HiroyasuSchool of Molecular Biosciences, Washington State University, Pullman, Washington, USA.
Zachary T ColburnSchool of Molecular Biosciences, Washington State University, Pullman, Washington, USA.
Rosa V VentrellaDepartment of Dermatology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Susan B HopkinsonSchool of Molecular Biosciences, Washington State University, Pullman, Washington, USA.
Omar SkalliDepartment of Biological Sciences, University of Memphis, Memphis, Tennessee, USA.
Jonathan C R JonesSchool of Molecular Biosciences, Washington State University, Pullman, Washington, USA. Electronic address: jcr.jones@vetmed.wsu.edu.
Washington State University · USNorthwestern University · USUniversity of Liverpool · GBUniversity of Memphis · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
Keratinocyte Migration and Wound HealingR01AR054184 · NIAMS · WASHINGTON STATE UNIVERSITY · PI JONES, JONATHAN C. · 2006 to 2015
$3.3M
Functional analyses of a member of a novel family of laminin-related proteinsK99AR060242 · NIAMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI HAMILL, KEVIN J · 2011 to 2012
$177k
NIAMS NIH HHS K99 AR060242NIAMS NIH HHS R01 AR054184NIGMS NIH HHS T32 GM008061
6 · The paper itself

Abstract

The migration of keratinocytes in wound healing requires coordinated activities of the motility machinery of a cell, the cytoskeleton, and matrix adhesions. In this study, we assessed the role of alpha actinin-1 (ACTN1), one of the two alpha actinin isoforms expressed in keratinocytes, in skin cell migration via a small hairpin RNA-mediated knockdown approach. Keratinocytes deficient in ACTN1 exhibit changes in their actin cytoskeleton organization, a loss in front-rear polarity, and impaired lamellipodial dynamics. They also display aberrant directed motility and move slower compared with their wild-type counterparts. Moreover, they have abnormally arranged matrix adhesion sites. Specifically, the focal adhesions in ACTN1 knockdown keratinocytes are not organized as distinct entities. Rather, focal adhesion proteins are arranged in a circle subjacent to cortical fibers of actin. In the same cells, hemidesmosome proteins arrange in cat paw patterns, more typical of confluent, stationary cells, and β4 integrin dynamics are reduced in knockdown cells compared with control keratinocytes. In summary, our data suggest a mechanism by which ACTN1 determines the motility of keratinocytes by regulating the organization of the actin cytoskeleton, focal adhesion, and hemidesmosome proteins complexes, thereby modulating cell speed, lamellipodial dynamics, and directed migration.

Indexed as

ActininActinsAdenoviridaeCell MovementCell SeparationCytoskeletonEpidermolysis Bullosa, JunctionalFlow CytometryHemidesmosomesHumansIntegrin beta4KeratinocytesPseudopodiaSkinWound HealingActininActinsIntegrin beta4

Identifiers

PMID25431851
PMCPMC4366307
OpenAlexW2008028433

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.