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Condensates of synaptic vesicles and synapsin are molecular beacons for actin sequestering and polymerization. | LitMetric

AI Article Synopsis

  • - Neuronal communication depends on the organization of synaptic vesicle (SV) clusters, which form through a process called liquid-liquid phase separation (LLPS) that involves synapsins, proteins that interact with actin.
  • - The study used advanced imaging techniques to explore how synapsins and SVs work together to organize the actin cytoskeleton in presynaptic regions, which is crucial for synaptic activity.
  • - Findings suggest that LLPS of synapsins triggers actin polymerization, leading to the proper arrangement of SV clusters along axons, providing insights into how these mechanisms support neurotransmission and subsequent behavioral functions.

Article Abstract

Neuronal communication relies on precisely maintained synaptic vesicle (SV) clusters, which assemble via liquid-liquid phase separation (LLPS). This process requires synapsins, the major synaptic phosphoproteins, which are known to bind actin. The reorganization of SVs, synapsins and actin is a hallmark of synaptic activity, but their interplay is still unclear. Here we combined the reconstitution approaches and super-resolution imaging to dissect the roles of synapsin-SV condensates in the organization of the presynaptic actin cytoskeleton. Our data indicate that LLPS of synapsin initiates actin polymerization, allowing for SV:synapsin:actin assemblies to facilitate the mesoscale organization of SV clusters along axons mimicking the native presynaptic organization in both lamprey and mammalian synapses. Understanding the relationship between the actin network and synapsin-SVs condensates is an essential building block on a roadmap to unravel how coordinated neurotransmission along the axon enables circuit function and behavior.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11275919PMC
http://dx.doi.org/10.1101/2024.07.19.604346DOI Listing

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