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The SNAP-25 Linker as an Adaptation Toward Fast Exocytosis We confirm that the palmitoylated linker-cysteines are important for membrane association A SNAP-25 mutant without cysteines supported exocytosis, but the fusion rate was slowed down and the fusion pore duration prolonged
Oxidation state of SNAP-25 and formation of adducts We demonstrate, using mass spectrometry, that sulfur-containing reducing agents form adducts with the cysteines Through CD spectrometry, we demonstrate differences in protein folding with temperature, oxidation state, and presence of adducts on SNAP-25
SNAP-25, a Known Presynaptic Protein with Emerging . . . SNAP-25 is a component of the SNARE complex, which is central to synaptic vesicle exocytosis, and, by directly interacting with different calcium channels subunits, it negatively modulates neuronal voltage-gated calcium channels, thus regulating intracellular calcium dynamics
SNAP-25, a Known Presynaptic Protein with Emerging . . . SNAP-25 is a component of the SNARE complex, which is central to synaptic vesicle exocytosis, and, by directly interacting with different calcium channels subunits, it negatively modulates neuronal voltage-gated calcium channels, thus regulating intracellular calcium dynamics
The SNARE protein SNAP-25 is required for normal exocytosis . . . We investigated the role of SNAP-25, a key component of this complex, in hearing, by generating and analyzing a conditional knockout mouse model allowing a targeted postnatal deletion of Snap-25 in IHCs