English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons133193

Sharma,  S.
Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons104871

Lindau,  M.
Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)

2514900_Suppl.pdf
(Supplementary material), 16MB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002E-8DFB-F
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.