Dissection of SNARE-driven membrane fusion and neuroexocytosis by wedging small hydrophobic molecules into the SNARE zipper

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Neuronal SNARE proteins mediate neurotransmitter release at the synapse by facilitating the fusion of vesicles to the presynaptic plasma membrane. Cognate v-SNAREs and t-SNAREs from the vesicle and the plasma membrane, respectively, zip up and bring about the apposition of two membranes attached at the C-terminal ends. Here, we demonstrate that SNARE zippering can be modulated in the midways by wedging with small hydrophobic molecules. Myricetin, which intercalated into the hydrophobic inner core near the middle of the SNARE complex, stopped SNARE zippering in motion and accumulated the trans-complex, where the N-terminal region of v-SNARE VAMP2 is in the coiled coil with the frayed C-terminal region. Delphinidin and cyanidin inhibited N-terminal nucleation of SNARE zippering. Neuronal SNARE complex in PC12 cells showed the same pattern of vulnerability to small hydrophobic molecules. We propose that the half-zipped trans-SNARE complex is a crucial intermediate waiting for a calcium trigger that leads to fusion pore opening.
Publisher
NATL ACAD SCIENCES
Issue Date
2010-12
Language
English
Article Type
Article
Keywords

SYNAPTIC VESICLE FUSION; ACETYLCHOLINE-RELEASE; PC12 CELLS; COMPLEX; EXOCYTOSIS; HEMIFUSION; INHIBITORS; PROTEINS; GP41; SYNAPTOBREVIN

Citation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.107, no.51, pp.22145 - 22150

ISSN
0027-8424
DOI
10.1073/pnas.1006899108
URI
http://hdl.handle.net/10203/97085
Appears in Collection
PH-Journal Papers(저널논문)
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