ArticleScientific reports2014
Synaptotagmin 1 and Ca2+ drive trans SNARE zippering.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- The evolution of organellar calcium mapping technologies.Cell calcium · 2022Review
- Elevation of gene expression of calcineurin, calmodulin and calsyntenin in oxidative stress induced PC12 cells.Genes & diseases · 2021Article
- TNF Production in Activated RBL-2H3 Cells Requires Munc13-4.Inflammation · 2020Article
- Going Too Far Is the Same as Falling ShortFrontiers in cellular neuroscience · 2019Review
- Diverse exocytic pathways for mast cell mediators.Biochemical Society transactions · 2018Review
- Liver X Receptor Agonist GW3965 Regulates Synaptic Function upon Amyloid Beta Exposure in Hippocampal Neurons.Neurotoxicity research · 2018Article
- Munc18a clusters SNARE-bearing liposomes prior toThe Biochemical journal · 2017Article
- A Stimulation Function of Synaptotagmin-1 in Ternary SNARE Complex Formation Dependent on Munc18 and Munc13.Frontiers in molecular neuroscience · 2017Article
- Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Frontiers in molecular neuroscience · 2017Review
- PI(4,5)P₂-binding effector proteins for vesicle exocytosis.Biochimica et biophysica acta · 2015Review
- Synaptotagmin-1 is an antagonist for Munc18-1 in SNARE zippering.The Journal of biological chemistry · 2015Article
- Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptotagmin 1 (Syt1) is a major Ca(2+)-sensor that evokes neurotransmitter release. Here we used site-specific fluorescence resonance energy transfer (FRET) assay to investigate the effects of Syt1 on SNAREpin assembly. C2AB, a soluble version of Syt1, had virtually no stimulatory effect on the rate of the FRET at N-terminus of SNARE complex both with and without Ca(2+), indicating C2AB does not interfere with the initial nucleation of SNARE assembly. However, C2AB-Ca(2+) accelerated the FRET rate significantly at membrane proximal region, indicating C2AB-Ca(2+) promotes the transition from a partially assembled SNARE complex to the fusion-competent SNAREpin. Similar enhancement was also observed at the end of the transmembrane domain of SNARE proteins. The stimulatory effect disappeared if there was no membrane or only neutral membrane present.
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Registered trials
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.