Evidence map›Paper›PMID 28852060›Full record

ArticleScientific reports2017

FMNL2 and -3 regulate Golgi architecture and anterograde transport downstream of Cdc42.

Frieda Kage, Anika Steffen, Adolf Ellinger, Carmen Ranftler, Christian Gehre, Cord Brakebusch, Margit Pavelka, Theresia Stradal, Klemens Rottner

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  3. Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024
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  17. Tuba Activates Cdc42 during Neuronal Polarization Downstream of the Small GTPase Rab8a.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 3 countries.

Frieda KageDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany.
Anika SteffenDepartment of Cell Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124, Braunschweig, Germany.
Adolf EllingerCenter for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstraße 17, 1090, Vienna, Austria.
Carmen RanftlerCenter for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstraße 17, 1090, Vienna, Austria.
Christian GehreDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany.
Cord BrakebuschBiomedical Institute, BRIC, University of Copenhagen, DK-2200, Copenhagen, Denmark.
Margit PavelkaCenter for Anatomy and Cell Biology, Medical University of Vienna, Schwarzspanierstraße 17, 1090, Vienna, Austria.
Theresia StradalDepartment of Cell Biology, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124, Braunschweig, Germany.
Klemens RottnerDivision of Molecular Cell Biology, Zoological Institute, Technische Universität Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany. k.rottner@tu-braunschweig.de.ORCID http://orcid.org/0000-0003-4244-4198
Helmholtz Centre for Infection Research · DEMedical University of Vienna · ATUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rho-family small GTPase Cdc42 localizes at plasma membrane and Golgi complex and aside from protrusion and migration operates in vesicle trafficking, endo- and exocytosis as well as establishment and/or maintenance of cell polarity. The formin family members FMNL2 and -3 are actin assembly factors established to regulate cell edge protrusion during migration and invasion. Here we report these formins to additionally accumulate and function at the Golgi apparatus. As opposed to lamellipodia, Golgi targeting of these proteins required both their N-terminal myristoylation and the interaction with Cdc42. Moreover, Golgi association of FMNL2 or -3 induced a phalloidin-detectable actin meshwork around the Golgi. Importantly, functional interference with FMNL2/3 formins by RNAi or CRISPR/Cas9-mediated gene deletion invariably induced Golgi fragmentation in different cell lines. Furthermore, absence of these proteins led to enlargement of endosomes as well as defective maturation and/or sorting into late endosomes and lysosomes. In line with Cdc42 - recently established to regulate anterograde transport through the Golgi by cargo sorting and carrier formation - FMNL2/3 depletion also affected anterograde trafficking of VSV-G from the Golgi to the plasma membrane. Our data thus link FMNL2/3 formins to actin assembly-dependent functions of Cdc42 in anterograde transport through the Golgi apparatus.

Indexed as

AnimalsBiomarkerscdc42 GTP-Binding ProteinCell LineEndosomesFluorescent Antibody TechniqueForminsGene ExpressionGene Knockdown TechniquesGolgi ApparatusIntracellular Signaling Peptides and ProteinsLysosomesMiceProtein BindingProteinsProtein TransportBiomarkerscdc42 GTP-Binding ProteinFMNL2 protein, mouseFMNL3 protein, mouseForminsIntracellular Signaling Peptides and ProteinsProteins

Identifiers

PMID28852060
PMCPMC5575334
OpenAlexW2746850238

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.