Evidence map›Paper›PMID 23665582›Full record

ArticleNature structural & molecular biology2013

Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.

Alf Honigmann, Geert van den Bogaart, Emilio Iraheta, H Jelger Risselada, Dragomir Milovanovic, Veronika Mueller, Stefan Müllar, Ulf Diederichsen, Dirk Fasshauer, Helmut Grubmüller and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
13.5field-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

166 citing papers in PubMed, 292 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Phosphatidylserine liposomes forFrontiers in immunology · 2026
    Article
  8. Article
  9. Article
  10. Synaptotagmin-1 serves as a primary ZnNature communications · 2025
    Article
  11. PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

106 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

14 authors at 4 institutions in 4 countries.

Alf HonigmannDepartment of Nanobiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Geert van den Bogaart
Emilio Iraheta
H Jelger Risselada
Dragomir Milovanovic
Veronika Mueller
Stefan Müllar
Ulf Diederichsen
Dirk Fasshauer
Helmut Grubmüller
Stefan W Hell
Christian Eggeling
Karin Kühnel
Reinhard Jahn
Max Planck Institute for Biophysical Chemistry · DEUniversity of Göttingen · DEUniversity of Lausanne · CHUniversity of Oxford · GB

Funding

Structural Dynamics of the Exocytotic Fusion Machine in Neurons.P01GM072694 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI KIESSLING, VOLKER · 2005 to 2021
$17.4M
Medical Research Council MR/K01577X/1NIGMS NIH HHS P01 GM072694
6 · The paper itself

Abstract

Synaptic-vesicle exocytosis is mediated by the vesicular Ca(2+) sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca(2+) through PIP2. This interaction allows both Ca(2+)-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca(2+) triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca(2+) influx bringing the vesicle membrane close enough for membrane fusion.

Indexed as

AnimalsCrystallography, X-RayExocytosisModels, BiologicalModels, MolecularPC12 CellsPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein ConformationRatsSynaptic VesiclesSynaptotagmin ISyntaxin 1Phosphatidylinositol 4,5-DiphosphateSynaptotagmin ISyntaxin 1Syt1 protein, rat

Identifiers

PMID23665582
PMCPMC3676452
OpenAlexW1978302530

What OpenQuestion holds

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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.