Evidence map›Paper›PMID 11114192›Full record

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

Role of the conserved WHXL motif in the C terminus of synaptotagmin in synaptic vesicle docking.

M Fukuda, J E Moreira, V Liu, M Sugimori, K Mikoshiba, R R Llinás

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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. SV2B is essential for the integrity of the glomerular filtration barrier.Laboratory investigation; a journal of technical methods and pathology · 2015
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Vesicular reuptake inhibition by a synaptotagmin I C2B domain antibody at the squid giant synapse.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  13. Dual roles of the C2B domain of synaptotagmin I in synchronizing Ca2+-dependent neurotransmitter release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  14. Synaptotagmin I synchronizes transmitter release in mouse hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  15. Review
  16. 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.

M FukudaLaboratory for Developmental Neurobiology, Brain Science Institute, The Institute of Physical and Chemical Research (RIKEN), Saitama 351-0198, Japan.
J E Moreira
V Liu
M Sugimori
K Mikoshiba
R R Llinás

Funding

VISUAL-VESTIBULAR INTERACTION IN EYE MOVEMENT CONTROLP01NS013742 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LLINAS, RODOLFO R · 1985 to 2011
$15.6M
NINDS NIH HHS NS 13742NINDS NIH HHS P01 NS013742
6 · The paper itself

Abstract

Synaptotagmin (Syt) I, an abundant synaptic vesicle protein, consists of one transmembrane region, two C2 domains, and a short C terminus. This protein is essential for both synaptic vesicle exocytosis and endocytosis via its C2 domains. Although the short C terminus is highly conserved among the Syt family and across species, little is known about the exact role of the conserved C terminus of Syt I. In this paper, we report a function of the Syt I C terminus in synaptic vesicle docking at the active zones. Presynaptic injection of a peptide corresponding to the C-terminal 21 amino acids of Syt I (named Syt-C) into the squid giant synapse blocked synaptic transmission without affecting the presynaptic action potential or the presynaptic Ca(2+) currents. The same procedure repeated with a mutant C-terminal peptide (Syt-CM) had no effect on synaptic transmission. Repetitive presynaptic stimulation with Syt-C produced a rapid decrease in the amplitude of the postsynaptic potentials as the synaptic block progressed, indicating that the peptide interferes with the docking step rather than the fusion step of synaptic vesicles. Electron microscopy of the synapses injected with the Syt-C peptide showed a marked decrease in the number of docked synaptic vesicles at the active zones, as compared with controls. These results indicate that Syt I is a multifunctional protein that is involved in at least three steps of synaptic vesicle cycle: docking, fusion, and reuptake of synaptic vesicles.

Indexed as

Calcium-Binding ProteinsAction PotentialsAmino Acid MotifsAmino Acid SequenceAnimalsCell MembraneConserved SequenceDecapodiformesMembrane GlycoproteinsMolecular Sequence DataNerve Tissue ProteinsPC12 CellsPeptidesPresynaptic TerminalsRatsStellate GanglionCalcium-Binding ProteinsMembrane GlycoproteinsNerve Tissue ProteinsPeptidesSynaptotagmins

Identifiers

PMID11114192
PMCPMC18984

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.