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Synaptotagmin-1–, Munc18-1–, and Munc13-1–dependent liposome fusion with a few neuronal SNAREs

Karolina P. Stepien, Josep Rizo

2021Proceedings of the National Academy of Sciences41 citationsDOIOpen Access PDF

Abstract

Significance Neurotransmitter release is crucial for neuronal communication. Reproducing the steps that lead to neuronal exocytosis with lipid vesicles and purified proteins provides a powerful strategy to elucidate the molecular mechanisms underlying release. Previous studies showed that reconstitution experiments including Munc18-1, Munc13-1, NSF, α-SNAP, and the SNARE proteins synaptobrevin, syntaxin-1, and SNAP-25, all of which are critical for neurotransmitter release, led to highly efficient vesicle fusion. However, synaptotagmin-1, the Ca 2+ sensor that triggers release, did not have detectable effects in these fusion assays. We now show that, when the amounts of synaptobrevin and syntaxin-1 are lowered in otherwise analogous reconstitution experiments, vesicle fusion is strongly dependent on synaptotagmin-1, exhibiting several features that parallel those of neurotransmitter release in neurons.

Topics & Concepts

Synaptotagmin 1ExocytosisSynaptobrevinVesicle fusionNeurotransmitterSyntaxinSynaptotagmin ICell biologySynaptic vesicleLipid bilayer fusionVesicleSTX1AChemistrySNAP25SNARE complexBiologyBiophysicsBiochemistryMembraneReceptorCellular transport and secretionLipid Membrane Structure and BehaviorCalcium signaling and nucleotide metabolism
Synaptotagmin-1–, Munc18-1–, and Munc13-1–dependent liposome fusion with a few neuronal SNAREs | Litcius