ArticlePLoS computational biology2017
An aggregation-removal model for the formation and size determination of post-synaptic scaffold domains.
Article in PLoS computational biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- DNA-PAINT resolves E-cadherin-independent cross-junctional F-actin organization in Drosophila embryonic tissue.Biophysical journal · 2026Article
- Cellular diffusion processes in singularly perturbed domains.Journal of mathematical biology · 2024Review
- Asymptotic analysis of particle cluster formation in the presence of anchoring sites.The European physical journal. E, Soft matter · 2024Article
- Stable but not rigid: Chronic in vivo STED nanoscopy reveals extensive remodeling of spines, indicating multiple drivers of plasticity.Science advances · 2021Article
- Reciprocal stabilization of glycine receptors and gephyrin scaffold proteins at inhibitory synapses.Biophysical journal · 2021Article
- The biophysical basis underlying the maintenance of early phase long-term potentiation.PLoS computational biology · 2021Article
- Activity Dependent and Independent Determinants of Synaptic Size Diversity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Computational Modeling of Inhibitory Transsynaptic Signaling in Hippocampal and Cortical Neurons Expressing Intrabodies Against Gephyrin.Frontiers in cellular neuroscience · 2020Article
- Inhibitory Receptor Diffusion Dynamics.Frontiers in molecular neuroscience · 2019Article
- Design and implementation of multi-signal and time-varying neural reconstructions.Scientific data · 2018Article
- Cooperative stochastic binding and unbinding explain synaptic size dynamics and statistics.PLoS computational biology · 2017Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation and stability of synapses are key questions in neuroscience. Post-synaptic domains have been classically conceived as resulting from local insertion and turnover of proteins at the synapse. However, insertion is likely to occur outside the post-synaptic domains and advances in single-molecule imaging have shown that proteins diffuse in the plane of the membrane prior to their accumulation at synapses. We quantitatively investigated this scenario using computer simulations and mathematical analysis, taking for definiteness the specific case of inhibitory synapse components, i.e., the glycine receptor (GlyR) and the associated gephyrin scaffolding protein. The observed domain sizes of scaffold clusters can be explained by a dynamic balance between the aggregation of gephyrin proteins diffusing while bound to GlyR and their turnover at the neuron membrane. We also predict the existence of extrasynaptic clusters with a characteristic size distribution that significantly contribute to the size fluctuations of synaptic domains. New super-resolution data for gephyrin proteins established the existence of extrasynaptic clusters the sizes of which are consistent with the model predictions in a range of model parameters. At a general level, our results highlight aggregation with removal as a non-equilibrium phase separation which produces structures of tunable size.
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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.