Evidence map›Paper›PMID 29887380›Full record

ArticleCell2018

A Flat BAR Protein Promotes Actin Polymerization at the Base of Clathrin-Coated Pits.

Leonardo Almeida-Souza, Rene A W Frank, Javier García-Nafría, Adeline Colussi, Nushan Gunawardana, Christopher M Johnson, Minmin Yu, Gillian Howard, Byron Andrews, Yvonne Vallis and 1 more

Abstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Chemical and Mechanical Regulation of Leukocyte Migration.Cold Spring Harbor perspectives in biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Spatial N-glycan rearrangement on αNature communications · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Endocytic Roles of Glycans on Proteins and Lipids.Cold Spring Harbor perspectives in biology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Article

3 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

11 authors.

Leonardo Almeida-SouzaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: lalmeida@mrc-lmb.cam.ac.uk.
Rene A W FrankMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Javier García-NafríaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Adeline ColussiMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Nushan GunawardanaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Christopher M JohnsonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Minmin YuMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Gillian HowardMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Byron AndrewsMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Yvonne VallisMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Harvey T McMahonMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. Electronic address: hmm@mrc-lmb.cam.ac.uk.

Funding

Medical Research Council MC_U105178795
6 · The paper itself

Abstract

Multiple proteins act co-operatively in mammalian clathrin-mediated endocytosis (CME) to generate endocytic vesicles from the plasma membrane. The principles controlling the activation and organization of the actin cytoskeleton during mammalian CME are, however, not fully understood. Here, we show that the protein FCHSD2 is a major activator of actin polymerization during CME. FCHSD2 deletion leads to decreased ligand uptake caused by slowed pit maturation. FCHSD2 is recruited to endocytic pits by the scaffold protein intersectin via an unusual SH3-SH3 interaction. Here, its flat F-BAR domain binds to the planar region of the plasma membrane surrounding the developing pit forming an annulus. When bound to the membrane, FCHSD2 activates actin polymerization by a mechanism that combines oligomerization and recruitment of N-WASP to PI(4,5)P

Indexed as

Actin CytoskeletonAdaptor Proteins, Vesicular TransportCarrier ProteinsCell MembraneClathrinClathrin-Coated VesiclesEndocytosisHeLa CellsHumansLiposomesMembrane ProteinsMicroscopy, FluorescenceModels, MolecularMutagenesis, Site-DirectedRNA InterferenceRNA, Small InterferingAdaptor Proteins, Vesicular TransportCarrier ProteinsClathrinFCHSD2 protein, humanITSN1 protein, humanLiposomesMembrane ProteinsRNA, Small InterferingWiskott-Aldrich Syndrome Protein, Neuronalactin cytoskeletonARP2/3BAR domainclathrin-mediated endocytosiscytoskeletal forcesFCHSD2intersectinmembrane deformationNervous WreckN-WASP activation

Identifiers

PMID29887380
PMCPMC6057269

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.