Evidence map›Paper›PMID 38724689›Full record

ArticleCommunications biology2024

BIN1 regulates actin-membrane interactions during IRSp53-dependent filopodia formation.

Laura Picas, Charlotte André-Arpin, Franck Comunale, Hugo Bousquet, Feng-Ching Tsai, Félix Rico, Paolo Maiuri, Julien Pernier, Stéphane Bodin, Anne-Sophie Nicot and 5 more

Abstract read
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In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. 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

15 authors.

Laura PicasInstitut de Recherche en Infectiologie de Montpellier (IRIM), University of Montpellier, CNRS UMR 9004, Montpellier, France. laura.picas@irim.cnrs.fr.ORCID 0000-0002-5619-5228
Charlotte André-ArpinInstitut de Recherche en Infectiologie de Montpellier (IRIM), University of Montpellier, CNRS UMR 9004, Montpellier, France.
Franck ComunaleCRBM, University of Montpellier, CNRS UMR 5237, Montpellier, France.
Hugo BousquetInstitut Curie, CNRS UMR 144, PSL Research University, Paris, France.
Feng-Ching TsaiInstitut Curie, CNRS UMR 168, PSL Research University, Paris, France.ORCID 0000-0002-6869-5254
Félix RicoAix-Marseille Université, U1325 INSERM, DyNaMo, Turing center for living systems, Marseille, France.ORCID 0000-0002-7757-8340
Paolo MaiuriDipartimento di Medicina Molecolare e Biotecnologie Mediche, Università degli Studi di Napoli Federico II, Naples, Italy.ORCID 0000-0001-5079-445X
Julien PernierUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), Gif-sur-Yvette, France.
Stéphane BodinCRBM, University of Montpellier, CNRS UMR 5237, Montpellier, France.
Anne-Sophie NicotGrenoble Alpes University, INSERM U1216, Grenoble Institut Neurosciences, Grenoble, France.
Jocelyn LaporteDepartment of Translational Medicine, IGBMC, U1258, UMR7104 Strasbourg University, Collège de France, Illkirch, France.ORCID 0000-0001-8256-5862
Patricia BassereauInstitut Curie, CNRS UMR 168, PSL Research University, Paris, France.ORCID 0000-0002-8544-6778
Bruno GoudInstitut Curie, CNRS UMR 144, PSL Research University, Paris, France.ORCID 0000-0003-1227-4159
Cécile Gauthier-Rouvière *CRBM, University of Montpellier, CNRS UMR 5237, Montpellier, France. cecile.gauthier@crbm.cnrs.fr.ORCID 0000-0002-8364-3882
Stéphanie Miserey *Institut Curie, CNRS UMR 144, PSL Research University, Paris, France. Stephanie.Miserey@curie.fr.ORCID 0000-0003-4994-0258

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-10-IDEX-0001-02 PSLAgence Nationale de la Recherche (French National Research Agency) ANR-10- LBX-0038Agence Nationale de la Recherche (French National Research Agency) ANR-13-BSV2-0004-01
6 · The paper itself

Abstract

Amphiphysin 2 (BIN1) is a membrane and actin remodeling protein mutated in congenital and adult centronuclear myopathies. Here, we report an unexpected function of this N-BAR domain protein BIN1 in filopodia formation. We demonstrated that BIN1 expression is necessary and sufficient to induce filopodia formation. BIN1 is present at the base of forming filopodia and all along filopodia, where it colocalizes with F-actin. We identify that BIN1-mediated filopodia formation requires IRSp53, which allows its localization at negatively-curved membrane topologies. Our results show that BIN1 bundles actin in vitro. Finally, we identify that BIN1 regulates the membrane-to-cortex architecture and functions as a molecular platform to recruit actin-binding proteins, dynamin and ezrin, to promote filopodia formation.

Indexed as

Adaptor Proteins, Signal TransducingNerve Tissue ProteinsNuclear ProteinsPseudopodiaTumor Suppressor ProteinsActinsAnimalsCell LineCell MembraneHeLa CellsHumansActinsAdaptor Proteins, Signal TransducingBAIAP2 protein, humanBaiap2 protein, mouseBin1 protein, mouseNerve Tissue ProteinsNuclear ProteinsTumor Suppressor Proteins

Identifiers

PMID38724689
PMCPMC11082164

What OpenQuestion holds

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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.