Evidence map›Paper›PMID 26469246›Full record

ArticleNature communications2015

IRSp53 senses negative membrane curvature and phase separates along membrane tubules.

Coline Prévost, Hongxia Zhao, John Manzi, Emmanuel Lemichez, Pekka Lappalainen, Andrew Callan-Jones, Patricia Bassereau

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 230 citations in OpenAlex.

  1. Article
  2. Review
  3. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
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  7. Building the bridges: molecular mechanisms of tunneling nanotube formation.Cellular and molecular life sciences : CMLS · 2026
    Review
  8. Article
  9. Review
  10. Review
  11. Biophysical modeling of membrane curvature generation and curvature sensing by the glycocalyx.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Membrane Tension Regulation is Required for Wound Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

41 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Coline PrévostInstitut Curie, Centre de Recherche, 75248 Paris Cedex 05, France.
Hongxia ZhaoInstitute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland.
John ManziInstitut Curie, Centre de Recherche, 75248 Paris Cedex 05, France.
Emmanuel LemichezINSERM, U1065, UNSA, Centre Méditerranéen de Médecine Moléculaire, C3M, 06204 Nice Cedex 3, France.ORCID http://orcid.org/0000-0001-9080-7761
Pekka LappalainenInstitute of Biotechnology, University of Helsinki, 00014 Helsinki, Finland.
Andrew Callan-JonesCNRS, Laboratoire Matière et Systèmes Complexes, UMR 7057, 75205 Paris Cedex 13, France.
Patricia BassereauInstitut Curie, Centre de Recherche, 75248 Paris Cedex 05, France.
Centre National de la Recherche Scientifique · FRUniversity of Helsinki · FIInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BAR domain proteins contribute to membrane deformation in diverse cellular processes. The inverted-BAR (I-BAR) protein IRSp53, for instance, is found on the inner leaflet of the tubular membrane of filopodia; however its role in the formation of these structures is incompletely understood. Here we develop an original assay in which proteins are encapsulated in giant unilamellar vesicles connected to membrane nanotubes. Our results demonstrate that I-BAR dimers sense negative membrane curvature. Experiment and theory reveal that the I-BAR displays a non-monotonic sorting with curvature, and expands the tube at high imposed tension while constricting it at low tension. Strikingly, at low protein density and tension, protein-rich domains appear along the tube. This peculiar behaviour is due to the shallow intrinsic curvature of I-BAR dimers. It allows constriction of weakly curved membranes coupled to local protein enrichment at biologically relevant conditions. This might explain how IRSp53 contributes in vivo to the initiation of filopodia.

Indexed as

Cell Line, TumorCell MembraneHumansNerve Tissue ProteinsPseudopodiaBAIAP2 protein, humanNerve Tissue Proteins

Identifiers

PMID26469246
PMCPMC4634128
OpenAlexW2270516315

What OpenQuestion holds

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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.