Evidence map›Paper›PMID 11245681›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001

Direct interaction of a brain voltage-gated K+ channel with syntaxin 1A: functional impact on channel gating.

O Fili, I Michaelevski, Y Bledi, D Chikvashvili, D Singer-Lahat, H Boshwitz, M Linial, I Lotan

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
  3. Syntaxin 1 SerScience advances · 2023
    Article
  4. Review
  5. ER-PM Contact Sites - SNARING Actors in Emerging Functions.Frontiers in cell and developmental biology · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Regulation of neuronal M-channel gating in an isoform-specific manner: functional interplay between calmodulin and syntaxin 1A.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Syntaxin 5 regulates the endoplasmic reticulum channel-release properties of polycystin-2.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  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 2 institutions in 1 country.

O FiliDepartment of Physiology and Pharmacology, Sackler School of Medicine, Tel-Aviv University, 69978 Ramat-Aviv, Israel.
I Michaelevski
Y Bledi
D Chikvashvili
D Singer-Lahat
H Boshwitz
M Linial
I Lotan
Tel Aviv University · ILHebrew University of Jerusalem · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Presynaptic voltage-gated K(+) (Kv) channels play a physiological role in the regulation of transmitter release by virtue of their ability to shape presynaptic action potentials. However, the possibility of a direct interaction of these channels with the exocytotic apparatus has never been examined. We report the existence of a physical interaction in brain synaptosomes between Kvalpha1.1 and Kvbeta subunits with syntaxin 1A, occurring, at least partially, within the context of a macromolecular complex containing syntaxin, synaptotagmin, and SNAP-25. The interaction was altered after stimulation of neurotransmitter release. The interaction with syntaxin was further characterized in Xenopus oocytes by both overexpression and antisense knock-down of syntaxin. Direct physical interaction of syntaxin with the channel protein resulted in an increase in the extent of fast inactivation of the Kv1.1/Kvbeta1.1 channel. Syntaxin also affected the channel amplitude in a biphasic manner, depending on its concentration. At low syntaxin concentrations there was a significant increase in amplitudes, with no detectable change in cell-surface channel expression. At higher concentrations, however, the amplitudes decreased, probably because of a concomitant decrease in cell-surface channel expression, consistent with the role of syntaxin in regulation of vesicle trafficking. The observed physical and functional interactions between syntaxin 1A and a Kv channel may play a role in synaptic efficacy and neuronal excitability.

Indexed as

Calcium-Binding ProteinsMembrane ProteinsPotassium Channels, Voltage-GatedAnimalsAntigens, SurfaceBrainCells, CulturedExocytosisIon Channel GatingKv1.1 Potassium ChannelMembrane GlycoproteinsMicroinjectionsNerve Tissue ProteinsNeurotransmitter AgentsOocytesPatch-Clamp TechniquesAntigens, SurfaceCalcium-Binding ProteinsKv1.1 Potassium ChannelMembrane GlycoproteinsMembrane ProteinsNerve Tissue ProteinsNeurotransmitter AgentsPotassium ChannelsPotassium Channels, Voltage-GatedProtein SubunitsRecombinant Fusion ProteinsRNA, MessengerSynaptosomal-Associated Protein 25SynaptotagminsSyntaxin 1

Identifiers

PMID11245681
PMCPMC6762600
OpenAlexW1892056601

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.