Evidence map›Paper›PMID 22644377›Full record

ArticleHistochemistry and cell biology2012

An apical actin-rich domain drives the establishment of cell polarity during cell adhesion.

Federico Galvagni, Cosima Tatiana Baldari, Salvatore Oliviero, Maurizio Orlandini

Abstract read
In one paragraph

Article in Histochemistry and cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
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  10. The Binding of CD93 to Multimerin-2 Promotes Choroidal Neovascularization.Investigative ophthalmology & visual science · 2020
    Article
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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

4 authors.

Federico GalvagniDipartimento di Biotecnologie, Università degli Studi di Siena, Via Fiorentina 1, 53100 Siena, Italy.
Cosima Tatiana Baldari
Salvatore Oliviero
Maurizio Orlandini

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the most important questions in cell biology concerns how cells reorganize after sensing polarity cues. In the present study, we describe the formation of an actin-rich domain on the apical surface of human primary endothelial cells adhering to the substrate and investigate its role in cell polarity. We used confocal immunofluorescence procedures to follow the redistribution of proteins required for endothelial cell polarity during spreading initiation. Activated Moesin, vascular endothelial cadherin and partitioning defective 3 were found to be localized in the apical domain, whereas podocalyxin and caveolin-1 were distributed along the microtubule cytoskeleton axis, oriented from the centrosome to the cortical actin-rich domain. Moreover, activated signaling molecules were localized in the core of the apical domain in tight association with filamentous actin. During cell attachment, loss of the apical domain by Moesin silencing or drug disruption of the actin cytoskeleton caused irregular cell spreading and mislocalization of polarity markers. In conclusion, our results suggest that the apical domain that forms during the spreading process is a structural organizer of cell polarity by regulating trafficking and activation of signaling proteins.

Indexed as

Cell PolarityActin CytoskeletonActinsAnimalsAntigens, CDCadherin 5CadherinsCell AdhesionCell Line, TumorEpithelial CellsHeLa CellsHumansHuman Umbilical Vein Endothelial CellsIntracellular Signaling Peptides and ProteinsMiceMice, Inbred BALB CActinsAntigens, CDCadherin 5CadherinsIntracellular Signaling Peptides and ProteinsMicrofilament ProteinsmoesinVitronectin

Identifiers

PMID22644377
PMCPMC3426669

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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.