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2017 ; 12
(4
): e0176235
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gab.com Text
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The influence of cell membrane and SNAP25 linker loop on the dynamics and
unzipping of SNARE complex
#MMPMID28426820
Shi Y
; Zhang Y
; Lou J
PLoS One
2017[]; 12
(4
): e0176235
PMID28426820
show ga
The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)
complex is composed of three neuronal proteins VAMP2, Syntaxin and SNAP25, which
plays a core role during the process of membrane fusion. The zipping assembly of
the SNARE complex releases energies and drives the vesicle and cell membrane into
close proximity. In this study, we use all-atom molecular dynamics simulations to
probe the dynamics of SNARE and its unzipping process in the context of membrane
at the atomistic details. Our results indicated that the NTD of SNARE core domain
is relatively more stable than CTD, which is in agreement with previous
experiments. More importantly, possible interactions between the linker loop (LL)
region of SNAP25 and VAMP2 are observed, suggests that the LL region may
facilitate VAMP2 binding and SNARE initiation. The forced unzipping of SNARE in
the presence of membrane and LL of SNAP25 reveals the possible pathway for energy
generation of SNARE zipping, provides information to understand how force may
regulate the cooperativity between the membrane and the SNARE complex.