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Signal Transduction At the Nerve-terminal Level - Role of the Phosphorylation of Synaptic Vesicle Proteins
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Synapsin-i, An Actin-binding Protein Regulating Synaptic Vesicle Traffic In the Nerve-terminal
No full textComputer modeling of synapsin I binding to synaptic vesicles and F-actin: implications for regulation of neurotransmitter release.
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The Transglutaminase Hypothesis For the Action of Tetanus Toxin
No full textTetanus toxin potently and almost irreversibly inhibits the release of neurotransmitters from nerve terminals. The toxin binds to and activates transglutaminase, a Ca2+-dependent enzyme that can form stable crosslinks between substrate proteins. Transglutaminase is present in nerve terminals and recognizes synapsin I, an abundant synaptic vesicle phosphoprotein involved in neurotransmission, as an excellent substrate. The neuroparalytic action of tetanus toxin might be due, at least in part, to the stimulation of synaptic transglutaminase and the consequent crosslinking of synapsin I
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