ArticleFrontiers in cellular neuroscience2024
Visualizing the trans-synaptic arrangement of synaptic proteins by expansion microscopy.
Article in Frontiers in cellular neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Sphingolipids associate with the chlamydial nucleoid and mark developmental transitions in Chlamydia trachomatis.Nature communications · 2026Article
- Resolving endogenous protein organization in cells with nanometer resolution.Nature communications · 2026Article
- Synaptic Cell Adhesion: A Functional Perspective.Advances in neurobiology · 2026Review
- Scales of Postsynaptic Nanostructure: Molecules, Nanoclusters, and Nanodomains.Advances in neurobiology · 2026Review
- Multicolor Super-resolution Fluorescence Imaging of Cells by Expansion Microscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High fidelity synaptic neurotransmission in the millisecond range is provided by a defined structural arrangement of synaptic proteins. At the presynapse multi-epitope scaffolding proteins are organized spatially at release sites to guarantee optimal binding of neurotransmitters at receptor clusters. The organization of pre- and postsynaptic proteins in trans-synaptic nanocolumns would thus intuitively support efficient information transfer at the synapse. Visualization of these protein-dense regions as well as the minute size of protein-packed synaptic clefts remains, however, challenging. To enable efficient labeling of these protein complexes, we developed post-gelation immunolabeling expansion microscopy combined with Airyscan super-resolution microscopy. Using ~8-fold expanded samples, Airyscan enables multicolor fluorescence imaging with 20-40 nm spatial resolution. Post-immunolabeling of decrowded (expanded) samples provides increased labeling efficiency and allows the visualization of trans-synaptic nanocolumns. Our approach is ideally suited to investigate the pathological impact on nanocolumn arrangement e.g., in limbic encephalitis with autoantibodies targeting trans-synaptic leucine-rich glioma inactivated 1 protein (LGI1).
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