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Motorneurons Require Cysteine String Protein-α to Maintain the Readily Releasable Vesicular Pool and Synaptic Vesicle Recycling

AuthorsRozas, José Luis; Gómez-Sánchez, L.; Mircheski, Josif; Linares-Clemente, P.; Nieto-González, J.; Vázquez, M. Eugenio; Luján, Rafael; Fernández-Chacón, Rafael
Issue Date2012
CitationNeuron 74(1): 151-165 (2012)
AbstractCysteine string protein-α (CSP-α) is a synaptic vesicle protein that prevents activity-dependent neurodegeneration by poorly understood mechanisms. We have studied the synaptic vesicle cycle at the motor nerve terminals of CSP-α knock-out mice expressing the synaptopHluorin transgene. Mutant nerve terminals fail to sustain prolonged release and the number of vesicles available to be released decreases. Strikingly, the SNARE protein SNAP-25 is dramatically reduced. In addition, endocytosis during the stimulus fails to maintain the size of the recycling synaptic vesicle pool during prolonged stimulation. Upon depolarization, the styryl dye FM 2-10 becomes trapped and poorly releasable. Consistently with the functional results, electron microscopy analysis revealed characteristic features of impaired synaptic vesicle recycling. The unexpected defect in vesicle recycling in CSP-α knock-out mice provides insights into understanding molecular mechanisms of degeneration in motor nerve terminals. Cysteine string protein-α (CSP-α) is a synaptic vesicle protein that prevents activity-dependent neurodegeneration. Rozas et al. have used synaptopHluorin imaging and electrophysiology to find alterations in synaptic vesicle priming and recycling at motor nerve terminals of CSP-α KO mice. © 2012 Elsevier Inc.
Identifiersdoi: 10.1016/j.neuron.2012.02.019
issn: 0896-6273
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