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• W3206705348 abstract "At mammalian glutamatergic synapses, most basic elements of synaptic transmission have been shown to be modulated by specific transsynaptic adhesion complexes. However, although crucial for synapse homeostasis, a physiological regulation of synaptic vesicle endocytosis by adhesion molecules has not been firmly established. The homophilic adhesion protein N-cadherin is localized at the peri-active zone, where the highly temperature-dependent endocytosis of vesicles occurs. Here, we demonstrate an important modulatory role of N-cadherin in endocytosis at near physiological temperature by synaptophysin-pHluorin imaging. Different modes of endocytosis including bulk endocytosis were dependent on N-cadherin expression and function. N-cadherin modulation might be mediated by actin filaments because actin polymerization ameliorated the knockout-induced endocytosis defect. Using super-resolution imaging, we found strong recruitment of N-cadherin to glutamatergic synapses upon massive vesicle release, which might in turn enhance vesicle endocytosis. This provides a novel, adhesion protein-mediated mechanism for efficient coupling of exo- and endocytosis." @default.
• W3206705348 created "2021-10-25" @default.
• W3206705348 creator A5015997170 @default.
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• W3206705348 date "2021-10-07" @default.
• W3206705348 modified "2023-09-24" @default.
• W3206705348 title "Transsynaptic N-Cadherin Adhesion Complexes Control Presynaptic Vesicle and Bulk Endocytosis at Physiological Temperature" @default.
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• W3206705348 doi "https://doi.org/10.3389/fncel.2021.713693" @default.
• W3206705348 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8573734" @default.
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• W3206705348 hasPublicationYear "2021" @default.
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