biostudies-literatureWeiss ANNational Science Foundation Science and Technology CenterNINDS NIH HHSNational Institutes of Healththe Nanobiotechnology CenterNIGMS NIH HHS921-929https://www.ebi.ac.uk/biostudies/studies/S-EPMC6400860biostudies-literatureUnknown116(5)The discharge of neurotransmitters from vesicles is a regulated process. Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interacting with other SNARE and associated proteins. Synaptobrevin-2 transmembrane domain is embedded into the vesicle lipid bilayer except for its last three residues. These residues are hydrophilic and constitute synaptobrevin-2 C-terminal flexible region. The residue Y113 of synaptobrevin-2 flexible region was mutated to lysine and glutamate. The effects of these mutations on the exocytotic process in chromaffin cells were assessed using capacitance measurements combined with amperometry and stimulation by flash photolysis of caged Ca²⁺. Both Y113E and Y113K mutations reduced the number of fusion-competent vesicles and redBiophysical journalSynaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.PMC6400860R01NS38200R01GM085808R01 NS038200R01 GM085808T32 GM007469T32GM007469ECS-9876771Weiss ANfalseSynaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.The discharge of neurotransmitters from vesicles is a regulated process. Synaptobrevin-2, a snap receptor (SNARE) protein, participates in this process by interacting with other SNARE and associated proteins. Synaptobrevin-2 transmembrane domain is embedded into the vesicle lipid bilayer except for its last three residues. These residues are hydrophilic and constitute synaptobrevin-2 C-terminal flexible region. The residue Y113 of synaptobrevin-2 flexible region was mutated to lysine and glutamate. The effects of these mutations on the exocytotic process in chromaffin cells were assessed using capacitance measurements combined with amperometry and stimulation by flash photolysis of caged Ca²⁺. Both Y113E and Y113K mutations reduced the number of fusion-competent vesicles and red2019-01-01T00:00:00Z2019 Mar2025-06-01T03:25:37.545Z2025-06-01T03:25:37.545ZS-EPMC64008603079587110.1016/j.bpj.2019.01.028