ArticleThe European physical journal. E, Soft matter2024
Vesicle condensation induced by synapsin: condensate size, geometry, and vesicle shape deformations.
Article in The European physical journal. E, Soft matter, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed, 7 citations in OpenAlex.
- Hydroxy acid conjugation to lipids increases structural and hydrolytic stability.Nature communications · 2026Article
- Synapsin shields a lipid monolayer from interactions with vesicles and associated structural rearrangements.Biophysical journal · 2026Article
- Lipid Composition Modulates Secondary Structure at the Biocondensate-Membrane Interface.bioRxiv : the preprint server for biology · 2026Article
- Physiological implications of phase separation in vesicle organization and trafficking.BMC biology · 2026Review
- Vesicle dynamics in synapsin-induced condensates by passive X-ray microrheology.Biophysical journal · 2026Article
- The synaptic vesicle cluster as a controller of pre- and postsynaptic structure and function.The Journal of physiology · 2025Review
- Condensates of synaptic vesicles and synapsin-1 mediate actin sequestering and polymerization.The EMBO journal · 2025Article
- Condensates of synaptic vesicles and synapsin are molecular beacons for actin sequestering and polymerization.bioRxiv : the preprint server for biology · 2025Article
- Morphology and intervesicle distances in condensates of synaptic vesicles and synapsin.Biophysical journal · 2024Article
- Lipid vesicle pools studied by passive X-ray microrheology.The European physical journal. E, Soft matter · 2023Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
Abstract
We study the formation of vesicle condensates induced by the protein synapsin, as a cell-free model system mimicking vesicle pool formation in the synapse. The system can be considered as an example of liquid-liquid phase separation (LLPS) in biomolecular fluids, where one phase is a complex fluid itself consisting of vesicles and a protein network. We address the pertinent question why the LLPS is self-limiting and stops at a certain size, i.e., why macroscopic phase separation is prevented. Using fluorescence light microscopy, we observe different morphologies of the condensates (aggregates) depending on the protein-to-lipid ratio. Cryogenic electron microscopy then allows us to resolve individual vesicle positions and shapes in a condensate and notably the size and geometry of adhesion zones between vesicles. We hypothesize that the membrane tension induced by already formed adhesion zones then in turn limits the capability of vesicles to bind additional vesicles, resulting in a finite condensate size. In a simple numerical toy model we show that this effect can be accounted for by redistribution of effective binding particles on the vesicle surface, accounting for the synapsin-induced adhesion zone.
Identifiers
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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.