Journal
FEBS LETTERS
Volume 587, Issue 1, Pages 67-72Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2012.11.002
Keywords
Exocytosis; Membrane fusion; Synaptobrevin; SNARE complex; Amperometry
Funding
- NIH [R01GM085808]
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Synaptobrevin 2 (Syb2), syntaxin (Sx1A), and SNAP-25, generate a force to induce fusion pore formation. The v-SNARE, Syb2, is anchored to the vesicle membrane by a single transmembrane domain. Here we show that 2 tryptophans (W89/W90) located in the juxtamembrane domain of Syb2, which stabilize the transmembrane (TM) domain position, control the ratio of spontaneous vs. stimulated membrane fusion events in chromaffin cells. Changing the 2 hydrophobic tryptophans to neutral alanines promotes spontaneous membrane fusion, faster transmitter release kinetics and complete release from individual vesicles. The results indicate that the two tryptophans act as a fusion clamp making fusion stimulus-dependent. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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