Multiple conformations of a single SNAREpin between two nanodisc membranes reveal diverse pre-fusion states
- Multiple conformations of a single SNAREpin between two nanodisc membranes reveal diverse pre-fusion states
- 신재일; Xiaochu Lou; 권대혁; 신년균
- EPR; nanodisc; single-molecule FRET; SNARE; trans-SNAREpin
- Issue Date
- The Biochemical journal
- VOL 459, NO 1, 95-102
- SNAREpins must be formed between two membranes to
allow vesicle fusion, a required process for neurotransmitter
release. Although its post-fusion structure has been well
characterized, pre-fusion conformations have been elusive.
We used single-molecule FRET and EPR to investigate the
SNAREpin assembled between two nanodisc membranes.
The SNAREpin shows at least three distinct dynamic states,
which might represent pre-fusion intermediates. Although the
N-terminal half above the conserved ionic layer maintains
a robust helical bundle structure, the membrane-proximal Cterminal
half shows high FRET, representing a helical bundle
(45%), low FRET, reflecting a frayed conformation (39%) or
mid FRET revealing an as-yet unidentified structure (16%). It
is generally thought that SNAREpins are trapped at a partially
zipped conformation in the pre-fusion state, and complete SNARE
(soluble N-ethylmaleimide-sensitive factor-attachment protein
receptor) assembly happens concomitantly with membrane
fusion. However, our results show that the complete SNARE
complex can be formed without membrane fusion, which suggests
that the complete SNAREpin formation could precede membrane
fusion, providing an ideal access to the fusion regulators such as
complexins and synaptotagmin 1.
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