期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 51, 页码 18440-18443出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b10677
关键词
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资金
- European Research Council (ERC) [ADG 322699]
- National Institutes of Health (NIH) [R21NS0882S3, R01GM121787]
The t-SNARE complex plays a central role in neuronal fusion. Its components, syntaxin-1 and SNAP25, are largely present in individual clusters and partially colocalize at the presumptive fusion site. How these protein clusters modify local lipid composition and membrane morphology is largely unknown. In this work, using coarse-grained molecular dynamics, the transmembrane domains (TMDs) of t-SNARE complexes are shown to form aggregates leading to formation of lipid nano domains, which are enriched in cholesterol, phosphatidylinositol 4,5-bisphosphate, and gangliosidic lipids. These nano-domains induce membrane curvature that would promote a closer contact between vesicle and plasma membrane.
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