Evidence map›Paper›PMID 10944231›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Ca2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin.

S Quetglas, C Leveque, R Miquelis, K Sato, M Seagar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 107 citations in OpenAlex.

  1. CaScience advances · 2025
    Article
  2. Article
  3. Article
  4. The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021
    Review
  5. Article
  6. Article
  7. Review
  8. v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018
    Review
  9. Article
  10. Intracellular Ca2+ signaling and preimplantation development.Advances in experimental medicine and biology · 2015
    Review
  11. Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
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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

5 authors at 1 institution in 1 country.

S QuetglasInstitut National de la Santé et de la Recherche Médicale Unité, Université de la Méditerrannée, Marseille, France.
C Leveque
R Miquelis
K Sato
M Seagar
Mitsubishi Group (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic core complex formation is an essential step in exocytosis, and assembly into a superhelical structure may drive synaptic vesicle fusion. To ascertain how Ca(2+) could regulate this process, we examined calmodulin binding to recombinant core complex components. Surface plasmon resonance and pull-down assays revealed Ca(2+)-dependent calmodulin binding (K(d) = 500 nM) to glutathione S-transferase fusion proteins containing synaptobrevin (VAMP 2) domains but not to syntaxin 1 or synaptosomal-associated protein of 25 kDa (SNAP-25). Deletion mutations, tetanus toxin cleavage, and peptide synthesis localized the calmodulin-binding domain to VAMP(77-94), immediately C-terminal to the tetanus toxin cleavage site (Q(76)-F(77)). In isolated synaptic vesicles, Ca(2+)/calmodulin protected native membrane-inserted VAMP from proteolysis by tetanus toxin. Assembly of a (35)S-SNAP-25, syntaxin 1 GST-VAMP(1-96) complex was inhibited by Ca(2+)/calmodulin, but assembly did not mask subsequent accessibility of the calmodulin-binding domain. The same domain contains a predicted phospholipid interaction site. SPR revealed calcium-independent interactions between VAMP(77-94) and liposomes containing phosphatidylserine, which blocked calmodulin binding. Circular dichroism spectroscopy demonstrated that the calmodulin/phospholipid-binding peptide displayed a significant increase in alphahelical content in a hydrophobic environment. These data provide insight into the mechanisms by which Ca(2+) may regulate synaptic core complex assembly and protein interactions with membrane bilayers during exocytosis.

Indexed as

Vesicular Transport ProteinsAmino Acid SequenceAnimalsAntigens, SurfaceBinding SitesCalciumCalmodulinCircular DichroismExocytosisLiposomesMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsPhosphatidylserinesPhospholipidsProtein BindingAntigens, SurfaceCalciumCalmodulinLiposomesMembrane ProteinsNerve Tissue ProteinsPhosphatidylserinesPhospholipidsRecombinant Fusion ProteinsR-SNARE ProteinsSNARE ProteinsSynaptosomal-Associated Protein 25Syntaxin 1Tetanus ToxinVesicular Transport Proteins

Identifiers

PMID10944231
PMCPMC16927
OpenAlexW2058310774

What OpenQuestion holds

Textmetadata
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.