期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 43, 页码 18463-18468出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1006727107
关键词
chromaffin cell; patch clamp capacitance measurement; caged calcium; amperometry; electrochemical detector array
资金
- National Institutes of Health [R01NS38200, R01GM085808, T32GM008267]
- Nanobiotechnology Center (a National Science Foundation Science and Technology Center) [ECS-9876771]
- Deutsche Forschungsgemeinschaft [SFB523-B16, SFB530-C10]
- Lundbeck Foundation
- EU [HEALTH-F2-2009-242167]
- Lundbeck Foundation [R28-2008-1976] Funding Source: researchfish
Neurotransmitter release is mediated by the SNARE proteins synaptobrevin II (sybII, also known as VAMP2), syntaxin, and SNAP-25, generating a force transfer to the membranes and inducing fusion pore formation. However, the molecular mechanism by which this force leads to opening of a fusion pore remains elusive. Here we show that the ability of sybII to support exocytosis is inhibited by addition of one or two residues to the sybII C terminus depending on their energy of transfer from water to the membrane interface, following a Boltzmann distribution. These results suggest that following stimulation, the SNARE complex pulls the C terminus of sybII deeper into the vesicle membrane. We propose that this movement disrupts the vesicular membrane continuity leading to fusion pore formation. In contrast to current models, the experiments suggest that fusion pore formation begins with molecular rearrangements at the intravesicular membrane leaflet and not between the apposed cytoplasmic leaflets.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据