한빛사 논문
Daehun Park1, Yumei Wu1,4, Sang-Eun Lee2,4, Goeun Kim2, Seonyoung Jeong2, Dragomir Milovanovic1,3, Pietro De Camilli1* & Sunghoe Chang2*
1Departments of Neuroscience and Cell Biology, Howard Hughes Medical Institute, Program in Cellular Neuroscience, Neurodegeneration and Repair, Kavli Institute for Neuroscience, Yale University School of Medicine, New Haven, CT 06510, USA. 2Department of Physiology and Biomedical Sciences, Seoul National University College of Medicine, Seoul 03080, South Korea. 3Laboratory of Molecular Neuroscience, German Center for Neurodegenerative Diseases (DZNE), Charitéplatz 1, 10117 Berlin, Germany.
4These authors contributed equally: Yumei Wu, Sang-Eun Lee.
*Corresponding author
Abstract
Clusters of tightly packed synaptic vesicles (SVs) are a defining feature of nerve terminals. While SVs are mobile within the clusters, the clusters have no boundaries consistent with a liquid phase. We previously found that purified synapsin, a peripheral SV protein, can assemble into liquid condensates and trap liposomes into them. How this finding relates to the physiological formation of SV clusters in living cells remains unclear. Here, we report that synapsin alone, when expressed in fibroblasts, has a diffuse cytosolic distribution. However, when expressed together with synaptophysin, an integral SV membrane protein previously shown to be localized on small synaptic-like microvesicles when expressed in non-neuronal cells, is sufficient to organize such vesicles in clusters highly reminiscent of SV clusters and with liquid-like properties. This minimal reconstitution system can be a powerful model to gain mechanistic insight into the assembly of structures which are of fundamental importance in synaptic transmission.
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