Evidence map›Paper›PMID 28627515›Full record

ArticleNature communications2017

Lipid-mediated PX-BAR domain recruitment couples local membrane constriction to endocytic vesicle fission.

Johannes Schöneberg, Martin Lehmann, Alexander Ullrich, York Posor, Wen-Ting Lo, Gregor Lichtner, Jan Schmoranzer, Volker Haucke, Frank Noé

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Review
  3. Subcellular Cartography of the Phosphoinositide Multiverse.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2026
    Review
  4. Article
  5. Review
  6. Inactivation of PI3K-C2α deregulates cell death pathways and sensitizes to endotoxic shock.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Phosphoinositides as membrane organizers.Nature reviews. Molecular cell biology · 2022
    Review
  18. Load adaptation by endocytic actin networks.Molecular biology of the cell · 2022
    Article
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Johannes SchönebergDepartment of Mathematics and Computer Science, Freie Universität Berlin, Berlin 14195, Germany.
Martin LehmannLeibniz-Institut für Molekulare Pharmakologie, Robert-Roessle-Straße 10, Berlin 13125, Germany.
Alexander UllrichDepartment of Mathematics and Computer Science, Freie Universität Berlin, Berlin 14195, Germany.
York PosorLeibniz-Institut für Molekulare Pharmakologie, Robert-Roessle-Straße 10, Berlin 13125, Germany.
Wen-Ting LoLeibniz-Institut für Molekulare Pharmakologie, Robert-Roessle-Straße 10, Berlin 13125, Germany.
Gregor LichtnerDepartment of Mathematics and Computer Science, Freie Universität Berlin, Berlin 14195, Germany.
Jan SchmoranzerLeibniz-Institut für Molekulare Pharmakologie, Robert-Roessle-Straße 10, Berlin 13125, Germany.
Volker HauckeLeibniz-Institut für Molekulare Pharmakologie, Robert-Roessle-Straße 10, Berlin 13125, Germany.
Frank NoéDepartment of Mathematics and Computer Science, Freie Universität Berlin, Berlin 14195, Germany.
Freie Universität Berlin · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Clathrin-mediated endocytosis (CME) involves membrane-associated scaffolds of the bin-amphiphysin-rvs (BAR) domain protein family as well as the GTPase dynamin, and is accompanied and perhaps triggered by changes in local lipid composition. How protein recruitment, scaffold assembly and membrane deformation is spatiotemporally controlled and coupled to fission is poorly understood. We show by computational modelling and super-resolution imaging that phosphatidylinositol 3,4-bisphosphate [PI(3,4)P

Indexed as

AnimalsBinding SitesCell MembraneChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsHeLa CellsHumansModels, TheoreticalNuclear ProteinsPhosphatidylinositol PhosphatesPhospholipidsProtein DomainsSorting NexinsSurface Plasmon ResonanceDynaminsNuclear Proteinsphosphatidylinositol 3,4-diphosphatePhosphatidylinositol PhosphatesPhospholipidsPI3KCA protein, humanSNX9 protein, humanSorting NexinsTranscription Factors

Identifiers

PMID28627515
PMCPMC5481832
OpenAlexW2708931810

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.