Evidence map›Paper›PMID 12145198›Full record

ArticleThe EMBO journal2002

Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis.

Stephanie Quetglas, Cecile Iborra, Nobuyuki Sasakawa, Luc De Haro, Konosuke Kumakura, Kazuki Sato, Christian Leveque, Michael Seagar

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-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

39 citing papers in PubMed, 118 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. Interplay between morphogen-directed positional information systems and physiological signaling.Developmental dynamics : an official publication of the American Association of Anatomists · 2020
    Review
  7. Article
  8. Copine-6 Binds to SNAREs and Selectively Suppresses Spontaneous Neurotransmission.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  9. v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018
    Review
  10. Review
  11. Morphine Antidependence ofEvidence-based complementary and alternative medicine : eCAM · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

8 authors at 1 institution in 1 country.

Stephanie QuetglasInstitut National de la Santé et de la Recherche Médicale Unité 464, Université de la Méditerranée, 13916 Marseille Cedex 20, France.
Cecile Iborra
Nobuyuki Sasakawa
Luc De Haro
Konosuke Kumakura
Kazuki Sato
Christian Leveque
Michael Seagar
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurotransmitter release involves the assembly of a heterotrimeric SNARE complex composed of the vesicle protein synaptobrevin (VAMP 2) and two plasma membrane partners, syntaxin 1 and SNAP-25. Calcium influx is thought to control this process via Ca(2+)-binding proteins that associate with components of the SNARE complex. Ca(2+)/calmodulin or phospholipids bind in a mutually exclusive fashion to a C-terminal domain of VAMP (VAMP(77-90)), and residues involved were identified by plasmon resonance spectroscopy. Microinjection of wild-type VAMP(77-90), but not mutant peptides, inhibited catecholamine release from chromaffin cells monitored by carbon fibre amperometry. Pre-incubation of PC12 pheochromocytoma cells with the irreversible calmodulin antagonist ophiobolin A inhibited Ca(2+)-dependent human growth hormone release in a permeabilized cell assay. Treatment of permeabilized cells with tetanus toxin light chain (TeNT) also suppressed secretion. In the presence of TeNT, exocytosis was restored by transfection of TeNT-resistant (Q(76)V, F(77)W) VAMP, but additional targeted mutations in VAMP(77-90) abolished its ability to rescue release. The calmodulin- and phospholipid-binding domain of VAMP 2 is thus required for Ca(2+)-dependent exocytosis, possibly to regulate SNARE complex assembly.

Indexed as

Vesicular Transport ProteinsAmino Acid SequenceAmino Acid SubstitutionAnimalsCalmodulinCatecholaminesCattleChromaffin CellsExocytosisHuman Growth HormoneHumansMacromolecular SubstancesMembrane ProteinsMetalloendopeptidasesMicroinjectionsMolecular Sequence DataCalmodulinCatecholaminesHuman Growth HormoneMacromolecular SubstancesMembrane ProteinsMetalloendopeptidasesophiobolin APeptide FragmentsPhospholipidsRecombinant Fusion ProteinsR-SNARE ProteinsSesterterpenesSNARE ProteinsSTX1A protein, humanStx1a protein, ratSyntaxin 1TerpenesTetanus ToxinVesicular Transport Proteinszinc-endopeptidase, tetanus neurotoxin

Identifiers

PMID12145198
PMCPMC126150
OpenAlexW2116411945

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.