Ouberai, MM and Wang, J and Swann, MJ and Galvagnion, C and Guilliams, T and Dobson, CM and Welland, ME (2013) α-synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling. J Biol Chem.Full text not available from this repository.
There is increasing evidence for the involvement of lipid membranes in both the functional and pathological properties of α-synuclein (α-Syn). Despite many investigations to characterize the binding of α-Syn to membranes, there is still a lack of understanding of the binding mode linking the properties of lipid membranes to α-Syn insertion into these dynamic structures. Using a combination of an optical biosensing technique and in situ atomic force microscopy, we show that the binding strength of α-Syn is related to the specificity of the lipid environment (the lipid chemistry and steric properties within a bilayer structure) and to the ability of the membranes to accommodate and remodel upon the interaction of α-Syn with lipid membranes. We show that this interaction results in the insertion of α-Syn into the region of the head groups, inducing a lateral expansion of lipid molecules that can progress to further bilayer remodeling such as membrane thinning and expansion of lipids out of the membrane plane. We provide new insights into the affinity of α-Syn for lipid packing defects found in vesicles of high curvature and in planar membranes with cone-shaped lipids and suggest a comprehensive model of the interaction between α-Syn and lipid bilayers. The ability of α-Syn to sense lipid packing defects and to remodel membrane structure supports its proposed role in vesicle trafficking.
|Uncontrolled Keywords:||Alpha-synuclein Atomic force microscopy Membrane bilayer Membrane biophysics Membrane structure dual polarization interferometry lipid packing defects membrane remodeling protein-lipid interactions|
|Depositing User:||Cron Job|
|Date Deposited:||12 Jun 2013 17:10|
|Last Modified:||16 Sep 2013 01:08|
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