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  t-SNARE transmembrane domain clustering modulates lipid organization and membrane curvature.

Sharma, S., & Lindau, M. (2017). t-SNARE transmembrane domain clustering modulates lipid organization and membrane curvature. Journal of the American Chemical Society, 139(51), 18440-18443. doi:10.1021/jacs.7b10677.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-8DFB-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-9B33-F
Genre: Journal Article

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2514900.pdf (Publisher version), 5MB
 
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 Creators:
Sharma, S.1, Author              
Lindau, M.1, Author              
Affiliations:
1Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1832294              

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 Abstract: 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 nanodomains, 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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Language(s): eng - English
 Dates: 2017-12-132017
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.7b10677
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 139 (51) Sequence Number: - Start / End Page: 18440 - 18443 Identifier: -