Results 11 to 20 of about 53,984 (298)
SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling. [PDF]
Front Mol Neurosci, 2021 Membrane fusion is a universal feature of eukaryotic protein trafficking and is mediated by the soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) family. SNARE proteins embedded in opposing membranes spontaneously assemble to drive membrane fusion and cargo exchange in vitro.
Sauvola CW, Littleton JT.
europepmc +5 more sources
Cell ReportsSummary: Efficient synaptic vesicle (SV) recycling is essential for sustaining synaptic transmission. While the multiple roles of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in SV recycling are well documented, presynaptic regulation of ...
Tomofumi Yoshida +7 more
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Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion. [PDF]
Membranes (Basel), 2023 Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as a Ca2+ sensor. In preparation for fusion, SVs become attached to the PM by the SNARE protein complex,
Bykhovskaia M.
europepmc +4 more sources
Disorders of synaptic vesicle fusion machinery [PDF]
Journal of Neurochemistry, 2020 AbstractThe revolution in genetic technology has ushered in a new age for our understanding of the underlying causes of neurodevelopmental, neuromuscular and neurodegenerative disorders, revealing that the presynaptic machinery governing synaptic vesicle fusion is compromised in many of these neurological disorders. This builds upon decades of research
Holly Melland +2 more
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Nature Structural & Molecular Biology, 2008 The core of the neurotransmitter release machinery is formed by SNARE complexes, which bring the vesicle and plasma membranes together and are key for fusion, and by Munc18-1, which controls SNARE-complex formation and may also have a direct role in fusion.
Josep, Rizo, Christian, Rosenmund
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Cell Reports, 2023 Summary: Neurotransmitter release requires assembly of the SNARE complex fusion machinery, with multiple SNARE-binding proteins regulating when and where synaptic vesicle fusion occurs.
Elizabeth A. Brija +3 more
doaj +1 more source
Synaptic Vesicle Fusion without SNARE Transmembrane Regions [PDF]
Developmental Cell, 2013 Diverse roles in membrane fusion have been proposed for the transmembrane regions (TMRs) of SNARE proteins, including formation of channel-like transmembrane pores. Reporting in Neuron, Zhou et al. (2013) show that lipid-anchored SNAREs lacking TMRs can support neurotransmitter release, suggesting that SNAREs function primarily as power engines that ...
Rizo, Josep, Xu, Junjie
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Research progress on vesicle cycle and neurological disorders
Journal of Pharmacy & Pharmaceutical Sciences, 2021 Neurons are special polarized cells whose synaptic vesicles release neurotransmitters into the synaptic cleft, acting on postsynaptic receptors and thus transmitting information from presynaptic to postsynaptic states.
Chengcheng Zhang, Li-Juan Zhu, Ce Chen
doaj +1 more source
Palmitoylation of the synaptic vesicle fusion machinery [PDF]
Journal of Neurochemistry, 2009 AbstractThe fusion of synaptic vesicles with the pre‐synaptic plasma membrane mediates the secretion of neurotransmitters at nerve terminals. This pathway is regulated by an array of protein–protein interactions. Of central importance are the soluble NSF (N‐ethylmaleimide‐sensitive factor) attachment protein receptor (SNARE) proteins syntaxin 1 and ...
Prescott, Gerald R +3 more
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Synaptotagmin 1 oligomers clamp and regulate different modes of neurotransmitter release [PDF]
, 2020 Release of neurotransmitters relies on submillisecond coupling of synaptic vesicle fusion to the triggering signal: AP-evoked presynaptic Ca2+ influx.
Bello, Oscar D. +9 more
core +3 more sources