Evidence map›Paper›PMID 29579104›Full record

ArticlePloS one2018

A Rac1-FMNL2 signaling module affects cell-cell contact formation independent of Cdc42 and membrane protrusions.

Hanna Grobe, Andrea Wüstenhagen, Christian Baarlink, Robert Grosse, Katharina Grikscheit

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.5field-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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. 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

5 authors at 1 institution in 1 country.

Hanna GrobeInstitute of Pharmacology, Biochemical-Pharmacological Center, Philipps-University of Marburg, Marburg, Germany.
Andrea WüstenhagenInstitute of Pharmacology, Biochemical-Pharmacological Center, Philipps-University of Marburg, Marburg, Germany.
Christian BaarlinkInstitute of Pharmacology, Biochemical-Pharmacological Center, Philipps-University of Marburg, Marburg, Germany.
Robert GrosseInstitute of Pharmacology, Biochemical-Pharmacological Center, Philipps-University of Marburg, Marburg, Germany.
Katharina GrikscheitInstitute of Pharmacology, Biochemical-Pharmacological Center, Philipps-University of Marburg, Marburg, Germany.ORCID 0000-0003-4582-2350
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

De novo formation of epithelial cell-cell contacts relies on actin-based protrusions as well as tightly controlled turnover of junctional actin once cells encounter each other and adhesion complexes assemble. The specific contributions of individual actin regulators on either protrusion formation or junctional actin turnover remain largely unexplored. Based on our previous findings of Formin-like 2 (FMNL2)-mediated control of junctional actin dynamics, we investigated its potential role in membrane protrusions and impact on newly forming epithelial contacts. CRISPR/Cas9-mediated loss of FMNL2 in human MCF10A cells combined with optogenetic control of Rac1 activity confirmed its critical function in the establishment of intercellular contacts. While lamellipodial protrusion rates remained unaffected, FMNL2 knockout cells were characterized by impaired filopodia formation similar to depletion of the Rho GTPase Cdc42. Silencing of Cdc42, however, failed to affect FMNL2-mediated contact formation. Hence, we propose a cell-cell contact-specific and Rac1-mediated function of FMNL2 entirely independent of Cdc42. Consistent with this, direct visualizations of native epithelial junction formation revealed a striking and specifically Rac1- and not Cdc42-dependent recruitment of FMNL2 to newly forming junctions as well as established cell-cell contacts within epithelial sheets.

Indexed as

cdc42 GTP-Binding ProteinCell Culture TechniquesCell DifferentiationCell LineCRISPR-Cas SystemsEpithelial CellsForminsHumansIntercellular JunctionsMicroscopy, ConfocalProteinsPseudopodiarac1 GTP-Binding ProteinRNA InterferenceRNA, Small InterferingSignal Transductioncdc42 GTP-Binding ProteinFMNL2 protein, humanForminsProteinsrac1 GTP-Binding ProteinRNA, Small Interfering

Identifiers

PMID29579104
PMCPMC5868805
OpenAlexW2790038689

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.