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. 2010 Nov 4;68(3):473-87.
doi: 10.1016/j.neuron.2010.09.019.

SNARE Protein Recycling by αSNAP and βSNAP Supports Synaptic Vesicle Priming

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SNARE Protein Recycling by αSNAP and βSNAP Supports Synaptic Vesicle Priming

Andrea Burgalossi et al. Neuron. .
Free article

Erratum in

  • Neuron. 2012 Feb 9;73(3):620

Abstract

Neurotransmitter release proceeds by Ca(2+)-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 Ca(2+) 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 Ca(2+) 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.

Comment in

  • Vesicle priming in a SNAP.
    Müller M, Davis GW. Müller M, et al. Neuron. 2010 Nov 4;68(3):324-6. doi: 10.1016/j.neuron.2010.10.022. Neuron. 2010. PMID: 21040835 Free PMC article.

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