Evidence map›Paper›PMID 20173762›Full record

ArticleNature structural & molecular biology2010

Molecular mechanism of the synaptotagmin-SNARE interaction in Ca2+-triggered vesicle fusion.

Marija Vrljic, Pavel Strop, James A Ernst, R Bryan Sutton, Steven Chu, Axel T Brunger

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. 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. Synaptotagmin-1 serves as a primary ZnNature communications · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Molecular and Spectroscopic Characterization of Green and Red Cyanine Fluorophores from the Alexa Fluor and AF Series*.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  7. Neuromodulator release in neurons requires two functionally redundant calcium sensors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  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

6 authors.

Marija VrljicDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, California, USA.
Pavel Strop
James A Ernst
R Bryan Sutton
Steven Chu
Axel T Brunger

Funding

STRUCTURE OF PROTEINS INVOLVED IN SYNAPTIC EXOCYTOSISR01MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2000 to 2025
$4.7M
Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Howard Hughes Medical InstituteNIMH NIH HHS R01 MH063105NIMH NIH HHS R01-MH63105NIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

In neurons, SNAREs, synaptotagmin and other factors catalyze Ca(2+)-triggered fusion of vesicles with the plasma membrane. The molecular mechanism of this process, especially the interaction between synaptotagmin and SNAREs, remains an enigma. Here we characterized this interaction by single-molecule fluorescence microscopy and crystallography. The two rigid Ca(2+)-binding domains of synaptotagmin 3 (Syt3) undergo large relative motions in solution. Interaction with SNARE complex amplifies a particular state of the two domains that is further enhanced by Ca(2+). This state is represented by the first SNARE-induced Ca(2+)-bound crystal structure of a synaptotagmin fragment containing both domains. The arrangement of the Ca(2+)-binding loops of this structure of Syt3 matches that of SNARE-bound Syt1, suggesting a conserved feature of synaptotagmins. The loops resemble the membrane-interacting loops of certain viral fusion proteins in the postfusion state, suggesting unexpected similarities between both fusion systems.

Indexed as

AnimalsCalciumCrystallography, X-RayFluorescence Resonance Energy TransferModels, BiologicalMolecular Dynamics SimulationMolecular Sequence DataProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRatsSNARE ProteinsSynaptotagmin ICalciumSNARE ProteinsSynaptotagmin I

Identifiers

PMID20173762
PMCPMC2928146

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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.