ArticleScientific reports2020
A minimalist model to measure interactions between proteins and synaptic vesicles.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 18 citations in OpenAlex.
- Geometry effects on protein mobility in a synapse.Biophysical journal · 2025Article
- One-step nanoscale expansion microscopy reveals individual protein shapes.Nature biotechnology · 2025Article
- Condensates of synaptic vesicles and synapsin-1 mediate actin sequestering and polymerization.The EMBO journal · 2025Article
- The involvement of the synaptic vesicle cycle in homocysteine induced neurotoxicity in vitro and in vivo.Scientific reports · 2025Article
- The role of RNA in the nanoscale organization of α-synuclein phase separation.NAR molecular medicine · 2025Article
- Condensates of synaptic vesicles and synapsin are molecular beacons for actin sequestering and polymerization.bioRxiv : the preprint server for biology · 2025Article
- Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells.International journal of molecular sciences · 2024Article
- Actin-nucleation promoting factor N-WASP influences alpha-synuclein condensates and pathology.Cell death & disease · 2024Article
- Defining a Lewy Body: Running Up the Hill of Shifting Definitions and Evolving Concepts.Journal of Parkinson's disease · 2024Review
- Trafficking proteins show limited differences in mobility across different postsynaptic spines.iScience · 2023Article
- A Light-Activatable Photocaged Variant of the Ultra-High Affinity ALFA-Tag Nanobody.Chembiochem : a European journal of chemical biology · 2022Article
- α-Synuclein in the Synaptic Vesicle Liquid Phase: Active Player or Passive Bystander?Frontiers in molecular biosciences · 2022Review
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Authors and funding
7 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein dynamics in the synaptic bouton are still not well understood, despite many quantitative studies of synaptic structure and function. The complexity of the synaptic environment makes investigations of presynaptic protein mobility challenging. Here, we present an in vitro approach to create a minimalist model of the synaptic environment by patterning synaptic vesicles (SVs) on glass coverslips. We employed fluorescence correlation spectroscopy (FCS) to measure the mobility of monomeric enhanced green fluorescent protein (mEGFP)-tagged proteins in the presence of the vesicle patterns. We observed that the mobility of all eleven measured proteins is strongly reduced in the presence of the SVs, suggesting that they all bind to the SVs. The mobility observed in these conditions is within the range of corresponding measurements in synapses of living cells. Overall, our simple, but robust, approach should enable numerous future studies of organelle-protein interactions in general.
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