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SNARE Protein Recycling by αSNAP and βSNAP Supports Synaptic Vesicle Priming

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Burgalossi,  Andrea
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jung,  SangYong
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Meyer,  Guido
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jockusch,  Wolf J.
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jahn,  Olaf
Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Taschenberger,  Holger       
Department of Membrane Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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Brose,  Nils
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons182371

Rhee,  Jeong Seop
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Burgalossi, A., Jung, S., Meyer, G., Jockusch, W. J., Jahn, O., Taschenberger, H., et al. (2010). SNARE Protein Recycling by αSNAP and βSNAP Supports Synaptic Vesicle Priming. Neuron, 68(3), 473-487. doi:10.1016/j.neuron.2010.09.019.


Cite as: https://hdl.handle.net/21.11116/0000-000B-4ECC-9
Abstract
Neurotransmitter release proceeds by Ca2+-triggered, SNARE-complex-dependent synaptic vesicle fusion. After fusion, the ATPase NSF and its cofactors α- and βSNAP disassemble SNARE complexes, thereby recycling individual SNAREs for subsequent fusion reactions. We examined the effects of genetic perturbation of α- and βSNAP expression on synaptic vesicle exocytosis, employing a new Ca2+ uncaging protocol to study synaptic vesicle trafficking, priming, and fusion in small glutamatergic synapses of hippocampal neurons. By characterizing this protocol, we show that synchronous and asynchronous transmitter release involve different Ca2+ sensors and are not caused by distinct releasable vesicle pools, and that tonic transmitter release is due to ongoing priming and fusion of new synaptic vesicles during high synaptic activity. Our analysis of α- and βSNAP deletion mutant neurons shows that the two NSF cofactors support synaptic vesicle priming by determining the availability of free SNARE components, particularly during phases of high synaptic activity.