ArticleScientific reports2015
Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Synaptotagmin-1 C2B domains cooperatively stabilize the fusion stalkChemical science · 2022Article
- Synaptotagmin-1 membrane binding is driven by the C2B domain and assisted cooperatively by the C2A domain.Scientific reports · 2020Article
- Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin.Nature communications · 2019Article
- Overexpression of Mitochondrial Ligases Reverses Rotenone-Induced Effects in aFrontiers in neuroscience · 2019Article
- Human transposons are an abundant supply of transcription factor binding sites and promoter activities in breast cancer cell lines.Mobile DNA · 2019Article
- α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking.The Biochemical journal · 2017Article
- Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Frontiers in molecular neuroscience · 2017Review
- Membrane Fusion Involved in Neurotransmission: Glimpse from Electron Microscope and Molecular Simulation.Frontiers in molecular neuroscience · 2017Review
- Article
- Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1.Molecular biology of the cell · 2016Article
- Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength.Nature structural & molecular biology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Synaptotagmin 1 (Syt1), a major Ca(2+) sensor in neuroexocytosis, utilizes SNARE- and membrane-binding to regulate vesicle fusion, a required process for neurotransmitter release at the synapse. However, the mechanism by which Syt1 orchestrates SNARE- and membrane- binding to control individual vesicle fusion steps is still unclear. In this study, we used a number of single vesicle assays that can differentiate intermediates of neuroexocytosis, to focus on Syt1 mutants that might impair Syt1-SNARE/PIP2 interaction, Ca(2+)-binding, or membrane penetration. Our results show that, although putative Syt1-SNARE/PIP2 coupling through the polybasic region of the C2B domain is critical for vesicle docking, its disruption does not affect content release. In contrast, Ca(2+)-binding and membrane-penetration mutants significantly reduce content release. Our results thus delineate multiple functions of Syt1 along the pathway of Ca(2+)-triggered exocytosis in unprecedented detail.
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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.