Evidence map›Paper›PMID 24979773›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Arf6 exchange factor EFA6 and endophilin directly interact at the plasma membrane to control clathrin-mediated endocytosis.

Sonia Boulakirba, Eric Macia, Mariagrazia Partisani, Sandra Lacas-Gervais, Frédéric Brau, Frédéric Luton, Michel Franco

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. The Guanine Exchange FactorJournal of fungi (Basel, Switzerland) · 2025
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  20. Recombinant protein ofOncotarget · 2017
    Article
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 2 institutions in 1 country.

Sonia BoulakirbaInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and.
Eric MaciaInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and.
Mariagrazia PartisaniInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and.
Sandra Lacas-GervaisCentre Commun de Microscopie Appliquée, Université de Nice Sophia Antipolis, 06103 Nice, France.
Frédéric BrauInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and.
Frédéric LutonInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and.
Michel FrancoInstitut de Pharmacologie Moléculaire et Cellulaire, Unité Mixte de Recherche 7275, Centre National de la Recherche Scientifique, Université de Nice Sophia Antipolis, 06560 Valbonne, France; and franco@ipmc.cnrs.fr.
Institut de Pharmacologie Moléculaire et Cellulaire · FRUniversité Côte d'Azur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Members of the Arf family of small G proteins are involved in membrane traffic and organelle structure. They control the recruitment of coat proteins, and modulate the structure of actin filaments and the lipid composition of membranes. The ADP-ribosylation factor 6 (Arf6) isoform and the exchange factor for Arf6 (EFA6) are known to regulate the endocytic pathway of many different receptors. To determine the molecular mechanism of the EFA6/Arf6 function in vesicular transport, we searched for new EFA6 partners. In a two-hybrid screening using the catalytic Sec7 domain as a bait, we identified endophilin as a new partner of EFA6. Endophilin contains a Bin/Amphiphysin/Rvs (BAR) domain responsible for membrane bending, and an SH3 domain responsible for the recruitment of dynamin and synaptojanin, two proteins involved, respectively, in the fission and uncoating of clathrin-coated vesicles. By using purified proteins, we confirmed the direct interaction, and identified the N-BAR domain as the binding motif to EFA6A. We showed that endophilin stimulates the catalytic activity of EFA6A on Arf6. In addition, we observed that the Sec7 domain competes with flat but not with highly curved lipid membranes to bind the N-BAR. In cells, expression of EFA6A recruits endophilin to EFA6A-positive plasma membrane ruffles, whereas expression of endophilin rescues the EFA6A-mediated inhibition of transferrin internalization. Overall, our results support a model whereby EFA6 recruits endophilin on flat areas of the plasma membrane to control Arf6 activation and clathrin-mediated endocytosis.

Indexed as

Adaptor Proteins, Signal TransducingADP-Ribosylation Factor 6Cell MembraneClathrinCloning, MolecularEndocytosisGuanine Nucleotide Exchange FactorsPolymerase Chain ReactionRecombinant ProteinsXanthenesAdaptor Proteins, Signal TransducingADP-Ribosylation Factor 6Arf6 protein, mouseClathrinGuanine Nucleotide Exchange FactorsPsd protein, mouseRecombinant ProteinsSh3gl2 protein, mouseTexas redXanthenesmembrane curvaturesmall GTP-binding proteinsvesicular trafficking

Identifiers

PMID24979773
PMCPMC4084483
OpenAlexW2137424240

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.