Evidence map›Paper›PMID 25941386›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Mechanical stimulation induces formin-dependent assembly of a perinuclear actin rim.

Xiaowei Shao, Qingsen Li, Alex Mogilner, Alexander D Bershadsky, G V Shivashankar

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
6.6field-weighted citation impact, top 3% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 148 citations in OpenAlex.

  1. Pooled it
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  15. ERM proteins support perinuclear actin rim formation.Frontiers in cell and developmental biology · 2025
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28 more citing papers are in PubMed but not listed here.

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

5 authors at 4 institutions in 4 countries.

Xiaowei ShaoMechanobiology Institute, National University of Singapore, 117411 Singapore;
Qingsen LiMechanobiology Institute, National University of Singapore, 117411 Singapore;
Alex MogilnerCourant Institute and Department of Biology, New York University, New York, NY 10012;
Alexander D BershadskyMechanobiology Institute, National University of Singapore, 117411 Singapore; Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel; alexander.bershadsky@weizmann.ac.il shiva.gvs@gmail.com.
G V ShivashankarMechanobiology Institute, National University of Singapore, 117411 Singapore; Department of Biological Sciences, National University of Singapore, 117543 Singapore; and FIRC Institute of Molecular Oncology, Milan 20139, Italy alexander.bershadsky@weizmann.ac.il shiva.gvs@gmail.com.
National University of Singapore · SGCourant Institute of Mathematical Sciences · USFIRC Institute of Molecular Oncology · ITWeizmann Institute of Science · IL

Funding

Modeling mitotic spindle assemblyR01GM068952 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI MOGILNER, ALEXANDER · 2003 to 2014
$4.4M
NIGMS NIH HHS GM068952NIGMS NIH HHS R01 GM068952
6 · The paper itself

Abstract

Cells constantly sense and respond to mechanical signals by reorganizing their actin cytoskeleton. Although a number of studies have explored the effects of mechanical stimuli on actin dynamics, the immediate response of actin after force application has not been studied. We designed a method to monitor the spatiotemporal reorganization of actin after cell stimulation by local force application. We found that force could induce transient actin accumulation in the perinuclear region within ∼ 2 min. This actin reorganization was triggered by an intracellular Ca(2+) burst induced by force application. Treatment with the calcium ionophore A23187 recapitulated the force-induced perinuclear actin remodeling. Blocking of actin polymerization abolished this process. Overexpression of Klarsicht, ANC-1, Syne Homology (KASH) domain to displace nesprins from the nuclear envelope did not abolish Ca(2+)-dependent perinuclear actin assembly. However, the endoplasmic reticulum- and nuclear membrane-associated inverted formin-2 (INF2), a potent actin polymerization activator (mutations of which are associated with several genetic diseases), was found to be important for perinuclear actin assembly. The perinuclear actin rim structure colocalized with INF2 on stimulation, and INF2 depletion resulted in attenuation of the rim formation. Our study suggests that cells can respond rapidly to external force by remodeling perinuclear actin in a unique Ca(2+)- and INF2-dependent manner.

Indexed as

Actin CytoskeletonAnimalsBiomechanical PhenomenaCalciumCell NucleusFluorescent Antibody TechniqueForminsImmunoblottingMechanotransduction, CellularMiceMicrofilament ProteinsMicroscopy, Atomic ForceNIH 3T3 CellsPhysical StimulationCalciumForminsINF2 protein, mouseMicrofilament Proteinscalciumforceforminmechanotransductionperinuclear actin rim

Identifiers

PMID25941386
PMCPMC4443368
OpenAlexW1547861484

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.