“The Discovery of the Principle of Membrane Fusion and Neurotransmitter Release”
نویسنده
چکیده
منابع مشابه
کلونینگ، بیان و تخلیص پروتئین SNAP-25
Background & Objectives:Clostridial neurotoxin inhibits neurotransmitter release by selective and specific intracellular proteolysis of synaptosomal associated protein of 25KDa (SNAP-25), synaptobrevin/VAMP-2 and syntaxin. SNAP-25 is one of the components that forms docking complex in synaptic ends. This protein is subtrate for botulinum neurotoxins types A,C, and E. Each of these toxin serotyp...
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Clostridium botulinum type A (BoNT/A) produces a neurotoxin recently found to be useful as an injectable drug for the treatment of abnormal muscle contractions. The catalytic domain of this toxin which is responsible for the main toxin activity is a zinc metalloprotease that inhibits the release of neurotransmitter mediators in neuromuscular junctions. A cell penetrating cationic peptide, Tat, ...
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The structure of the core of the neuronal 'SNARE complex', involved in neurotransmitter release, has been determined recently. Its topological similarity to viral fusion proteins suggests how the SNARE complex might facilitate membrane fusion.
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Synaptotagmin 1 (Syt1) is a synaptic vesicle integral membrane protein that regulates neurotransmitter release by activating fast synchronous fusion and suppressing slower asynchronous release. The cytoplasmic C2 domains of Syt1 interact with SNAREs and plasma membrane phospholipids in a Ca(2+)-dependent manner and can substitute for full-length Syt1 in in vitro membrane fusion assays. To deter...
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Communication between neurons relies on chemical synapses and the release of neurotransmitters into the synaptic cleft. Neurotransmitter release is an exquisitely regulated membrane fusion event that requires the linking of an electrical nerve stimulus to Ca(2+) influx, which leads to the fusion of neurotransmitter-filled vesicles with the cell membrane. The timing of neurotransmitter release i...
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