ArticleFEBS letters2019
Symmetrical organization of proteins under docked synaptic vesicles.
Article in FEBS letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed.
- Turbocharging synaptic transmission: 12 SNAREpins are required for rapid release of reconstituted synaptic vesicles.Science advances · 2026Article
- SNAP-25 disease variants affect synaptic transmission by destabilizing SNARE complexes within a multimeric SNARE ring.Cell reports · 2026Article
- Assessing the Potential of NGF-Differentiated PC12 Cells as a Model for Synaptic Transmission.Molecular neurobiology · 2025Article
- Phosphorylation of SNAP-25 at Ser187 is enhanced following its cleavage by Botulinum Neurotoxin Serotype A, promoting the dominant-negative effect of the resulting fragment.PLoS pathogens · 2025Article
- Neuronal synaptic architecture revealed by cryo-correlative light and electron microscopy.Biophysics reports · 2025Article
- Using multiscale molecular dynamics simulations to explore the fusion machinery underlying neurotransmitter release.Quarterly reviews of biophysics · 2025Review
- Quantitative single-molecule analysis of assembly and CaCommunications biology · 2024Article
- Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization.The Journal of cell biology · 2024Article
- Exploring the structural dynamics of the vesicle priming machinery.Biochemical Society transactions · 2024Review
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- Synaptophysin chaperones the assembly of 12 SNAREpins under each ready-release vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- In situ architecture of the lipid transport protein VPS13C at ER-lysosome membrane contacts.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- Symmetrical arrangement of proteins under release-ready vesicles in presynaptic terminals.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Nascent fusion pore opening monitored at single-SNAREpin resolution.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
During calcium-regulated exocytosis, the constitutive fusion machinery is 'clamped' in a partially assembled state until synchronously released by calcium. The protein machinery involved in this process is known, but the supra-molecular architecture and underlying mechanisms are unclear. Here, we use cryo-electron tomography analysis in nerve growth factor-differentiated neuro-endocrine (PC12) cells to delineate the organization of the release machinery under the docked vesicles. We find that exactly six exocytosis modules, each likely consisting of a single SNAREpin with its bound Synaptotagmins, Complexin, and Munc18 proteins, are symmetrically arranged at the vesicle-PM interface. Mutational analysis suggests that the symmetrical organization is templated by circular oligomers of Synaptotagmin. The observed arrangement, including its precise radial positioning, is in-line with the recently proposed 'buttressed ring hypothesis'.
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