Source Data for: Nanoscale Architecture of Synaptic Vesicles and Scaffolding Complexes Revealed by Cryo-Electron Tomography
Abstract/Contents
- Abstract
- The spatial distribution of proteins and their arrangement within the cellular ultrastructure regulates the opening of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors in response to glutamate release at the synapse. Fluorescence microscopy imaging revealed that the postsynaptic density (PSD) and scaffolding proteins in the presynaptic active zone (AZ) align across the synapse to form a trans-synaptic “nanocolumn”, but the relation to synaptic vesicle release sites is uncertain. Here, we employ focused-ion beam (FIB) milling and cryo-electron tomography (cryo-ET) to image synapses under near-native conditions. Improved image contrast, enabled by FIB-milling, allows simultaneous visualization of supramolecular nanoclusters within the AZ and PSD and synaptic vesicles. Surprisingly, membrane-proximal synaptic vesicles, which fuse to release glutamate, are not preferentially aligned with AZ or PSD nanoclusters. These synaptic vesicles are linked to the membrane by peripheral protein densities, often consistent in size and shape with Munc13, as well as globular densities bridging the synaptic vesicle and plasma membrane, consistent with prefusion complexes of SNAREs, synaptotagmins, and complexin. Monte Carlo simulations of synaptic transmission events using bio-realistic models guided by our tomograms predict that clustering AMPARs within PSD nanoclusters increases the variability of the postsynaptic response but not its average amplitude. Together, our data support a model in which synaptic strength is tuned at the level of single vesicles by the spatial relationship between scaffolding nanoclusters and single synaptic vesicle fusion sites.
Description
| Type of resource | Dataset, three dimensional object |
|---|---|
| Date created | May 31, 2024 |
| Publication date | June 1, 2024; May 31, 2024 |
Creators/Contributors
| Author | Brunger, Axel |
https://orcid.org/0000-0001-5121-2036
(unverified)
|
|---|---|---|
| Author | Held, Richard |
https://orcid.org/0000-0001-8231-0341
(unverified)
|
Subjects
| Subject | synapse |
|---|---|
| Subject | tomography |
| Subject | MCell simulation |
| Genre | Data |
| Genre | 3d model |
| Genre | Data sets |
| Genre | Dataset |
| Genre | Three-dimensional scan |
Bibliographic information
| Related item | |
|---|---|
| DOI | https://doi.org/10.25740/xq706xv7995, https://doi.org/10.25740/xq706xv7995 |
| Location | https://purl.stanford.edu/xq706xv7995 |
Access conditions
- Use and reproduction
- User agrees that, where applicable, content will not be used to identify or to otherwise infringe the privacy or confidentiality rights of individuals. Content distributed via the Stanford Digital Repository may be subject to additional license and use restrictions applied by the depositor.
- License
- This work is licensed under a Creative Commons Attribution 4.0 International license (CC BY).
Preferred citation
- Preferred citation
- Brunger, A. (2024). Source Data for: Nanoscale Architecture of Synaptic Vesicles and Scaffolding Complexes Revealed by Cryo-Electron Tomography. Stanford Digital Repository. Available at https://purl.stanford.edu/xq706xv7995. https://doi.org/10.25740/xq706xv7995.
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Stanford Research Data
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