Evidence map›Paper›PMID 33568632›Full record

ArticleNature communications2021

The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.

Wing K Man, Bogachan Tahirbegi, Michail D Vrettas, Swapan Preet, Liming Ying, Michele Vendruscolo, Alfonso De Simone, Giuliana Fusco

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
6.6field-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

77 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Ion- and Temperature-Programmable Reconfiguration of Subcompartments in Synthetic Cells.Chembiochem : a European journal of chemical biology · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Lipid-packing defects are sufficient to modulate membrane insertion and the bound state of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  13. Article
  14. Review
  15. Article
  16. MicroRNAs and synaptic dysfunction in Parkinson's disease.Molecular therapy. Nucleic acids · 2025
    Review
  17. Article
  18. Review
  19. Article
  20. Article

17 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

8 authors at 4 institutions in 2 countries.

Wing K ManCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Bogachan TahirbegiDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK.
Michail D VrettasDepartment of Pharmacy, University of Naples "Federico II", Naples, 80131, Italy.ORCID http://orcid.org/0000-0002-5456-3226
Swapan PreetCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.
Liming YingNational Heart and Lung Institute, Imperial College London, Molecular Sciences Research Hub, White City Campus, London, W12 0BZ, UK.ORCID http://orcid.org/0000-0001-9752-6292
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK.ORCID http://orcid.org/0000-0002-3616-1610
Alfonso De SimoneDepartment of Pharmacy, University of Naples "Federico II", Naples, 80131, Italy. alfonso.desimone@unina.it.ORCID http://orcid.org/0000-0001-8789-9546
Giuliana FuscoCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, UK. gf203@cam.ac.uk.
University of Cambridge · GBImperial College London · GBFederico II University Hospital · ITUniversity of Naples Federico II · IT

Funding

Medical Research Council MR/N000676/1Medical Research Council MR/R000255/1
6 · The paper itself

Abstract

α-Synuclein (αS) is a presynaptic disordered protein whose aberrant aggregation is associated with Parkinson's disease. The functional role of αS is still debated, although it has been involved in the regulation of neurotransmitter release via the interaction with synaptic vesicles (SVs). We report here a detailed characterisation of the conformational properties of αS bound to the inner and outer leaflets of the presynaptic plasma membrane (PM), using small unilamellar vesicles. Our results suggest that αS preferentially binds the inner PM leaflet. On the basis of these studies we characterise in vitro a mechanism by which αS stabilises, in a concentration-dependent manner, the docking of SVs on the PM by establishing a dynamic link between the two membranes. The study then provides evidence that changes in the lipid composition of the PM, typically associated with neurodegenerative diseases, alter the modes of binding of αS, specifically in a segment of the sequence overlapping with the non-amyloid component region. Taken together, these results reveal how lipid composition modulates the interaction of αS with the PM and underlie its functional and pathological behaviours in vitro.

Indexed as

alpha-SynucleinHumansLipid MetabolismLipidsProtein ConformationSynaptic MembranesSynaptic Vesiclesalpha-SynucleinLipids

Identifiers

PMID33568632
PMCPMC7876145
OpenAlexW3128718664

What OpenQuestion holds

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LicenceCC BY
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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.