Evidence map›Paper›PMID 10737807›Full record

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

Direct interaction between synaptotagmin and the intracellular loop I-II of neuronal voltage-sensitive sodium channels.

B Sampo, N Tricaud, C Leveque, M Seagar, F Couraud, B Dargent

Abstract 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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  11. Physical and functional interaction between the dopamine transporter and the synaptic vesicle protein synaptogyrin-3.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
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  19. Direct interaction of a brain voltage-gated K+ channel with syntaxin 1A: functional impact on channel gating.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    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

6 authors at 1 institution in 1 country.

B SampoInstitut National de la Santé et de la Recherche Médicale, U464, Institut Jean Roche, Université de la Méditerranée, Boulevard P. Dramard, 13916 Marseille Cedex 20, France.
N Tricaud
C Leveque
M Seagar
F Couraud
B Dargent
Institut de Neurobiologie de la Méditerranée · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptotagmin, a synaptic vesicle protein involved in Ca(2+)-regulated exocytosis, displayed direct high affinity interaction with neuronal sodium channels. Monoclonal antibodies directed against synaptotagmins I and II adsorbed in a concentration-dependent and -specific manner [(3)H]saxitoxin prelabeled sodium channels extracted with detergent from nerve endings. Conversely, co-immunoprecipitation of synaptotagmin was achieved by antibodies against sodium channel subunits. Consistent with the co-immunoprecipitation assays, solubilized [(3)H]saxitoxin-prelabeled sodium channels were trapped on immobilized maltose binding protein (MBP)-synaptotagmin I. In vitro recombinant protein assays were employed to identify the interaction site of synaptotagmin I, which was located on the cytoplasmic loop between domains I and II of the sodium channel alphaIIA subunit. The co-immunoprecipitated synaptotagmin-sodium channel complexes were found to be Ca(2+)-dependent; this effect was mimicked by Ba(2+) and Sr(2+) but not Mg(2+). Finally the complex was shown to be distinct from the synaptotagmin-SNARE protein complex that can selectively interact with presynaptic calcium channels (N and P/Q types). Thus, our findings demonstrate an unexpected and direct interaction between sodium channels and synaptotagmin. The Ca(2+)-regulated association between sodium channels and a protein implicated in vesicular fusion may have intriguing consequences for the establishment and regulation of neuronal excitability.

Indexed as

Calcium-Binding ProteinsAnimalsCalciumIon Channel GatingMembrane GlycoproteinsNerve Tissue ProteinsNeuronsPrecipitin TestsRatsRecombinant Fusion ProteinsSodium ChannelsSynaptotagmin ISynaptotagminsCalciumCalcium-Binding ProteinsMembrane GlycoproteinsNerve Tissue ProteinsRecombinant Fusion ProteinsSodium ChannelsSynaptotagmin ISynaptotagminsSyt1 protein, rat

Identifiers

PMID10737807
PMCPMC16297
OpenAlexW2028656676

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.