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2015 ; 17
(24
): 15561-8
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Biophysics of ?-synuclein induced membrane remodelling
#MMPMID25665896
Shi Z
; Sachs JN
; Rhoades E
; Baumgart T
Phys Chem Chem Phys
2015[Jun]; 17
(24
): 15561-8
PMID25665896
show ga
?-Synuclein is an intrinsically disordered protein whose aggregation is a
hallmark of Parkinson's disease. In neurons, ?-synuclein is thought to play
important roles in mediating both endo- and exocytosis of synaptic vesicles
through interactions with either the lipid bilayer or other proteins. Upon
membrane binding, the N-terminus of ?-synuclein forms a helical structure and
inserts into the hydrophobic region of the outer membrane leaflet. However,
membrane structural changes induced by ?-synuclein are still largely unclear.
Here we report a substantial membrane area expansion induced by the binding of
?-synuclein monomers. This measurement is accomplished by observing the increase
of membrane area during the binding of ?-synuclein to pipette-aspirated giant
vesicles. The extent of membrane area expansion correlates linearly with the
density of ?-synuclein on the membrane, revealing a constant area increase
induced by the binding per ?-synuclein molecule. The area expansion per synuclein
is found to exhibit a strong dependence on lipid composition, but is independent
of membrane tension and vesicle size. Fragmentation or tubulation of the membrane
follows the membrane expansion process. However, contrary to BAR domain proteins,
no distinct tubulation-transition density can apparently be identified for
?-synuclein, suggesting a more complex membrane curvature generation mechanism.
Consideration of ?-synuclein's membrane binding free energy and biophysical
properties of the lipid bilayer leads us to conclude that membrane expansion by
?-synuclein results in thinning of the bilayer. These membrane thinning and
tubulation effects may underlie ?-synuclein's role in mediating cell trafficking
processes such as endo- and exocytosis.