Protein Phosphorylation in Depolarized Synaptosomes: Dissecting Primary Effects of Calcium from Synaptic Vesicle Cycling
Ivan Silbern, Kuan‐Ting Pan, Maksims Fiošins, Stefan Bonn, Silvio O. Rizzoli, Eugenio F. Fornasiero, Henning Urlaub, Reinhard Jahn
Abstract
Analysis of protein phosphorylation in isolated nerve terminals (synaptosomes) treated with C. botulinum neurotoxins (BoNT) to inhibit synaptic vesicle (SV) cycling reveals phosphorylation events that are primarily dependent on depolarization-induced Ca 2+ influx and those that also require active SV-cycling machinery. In particular, SV-cycling-dependent phosphorylation sites on synaptobrevin (Vamp2), syntaxin-1 (Stx1a), and cannabinoid receptor-1 (Cnr1) are capable of changing the rate of exo-and endocytosis in cultured hippocampal neurons.
Topics & Concepts
Synaptic vesicleDepolarizationExocytosisNeurotransmissionCell biologySynaptic vesicle recyclingChemistryPhosphorylationSNAP25Synaptic augmentationBulk endocytosisSTX1ASynaptic fatigueCalciumBiologySyntaxinBiophysicsBiochemistryVesicleReceptorMembraneOrganic chemistryCellular transport and secretionNeuroscience and Neuropharmacology ResearchLipid Membrane Structure and Behavior