SNARE zippering is hindered by polyphenols in the neuron
- SNARE zippering is hindered by polyphenols in the neuron
- 양유수; 김세현; 허바울; 공병재; 신종혁; 정영훈; 윤기정; 정우재; 신년균; 권대혁
- SNARE; polyphenol; PC12; zippering; Membrane fusion; Botulinum toxin; Neurotransmitter; FRET
- Issue Date
- Biochemical and biophysical research communications
- VOL 450, NO 1, 831-836
- Fusion of synaptic vesicles with the presynaptic plasma membrane in the neuron is mediated by soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE) proteins. SNARE complex formation is a zippering-like process which initiates at the N-terminus and proceeds to the C-terminal membrane-proximal region. Previously, we showed that this zippering-like process is regulated by several polyphenols, leading to the arrest of membrane fusion and the inhibition of neuroexocytosis. In vitro studies using purified SNARE proteins reconstituted in liposomes revealed that each polyphenol uniquely regulates SNARE zippering. However, the unique regulatory effect of each polyphenol in cells has not yet been examined. In the present study, we observed SNARE zippering in neuronal PC12 cells by measuring the fluorescence resonance energy transfer (FRET) changes of a cyan fluorescence protein (CFP) and a yellow fluorescence protein (YFP) fused to the N-termini or C-termini of SNARE proteins. We show that delphinidin and cyanidin inhibit the initial N-terminal nucleation of SNARE complex formation in a Ca2+-independent manner, while myricetin inhibits Ca2+-dependent transmembrane domain association of the SNARE complex in the cell. This result explains how polyphenols exhibit botulinum neurotoxin-like activity in vivo.
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