Complexin splits the membrane-proximal region of a single SNAREpin

作者：Yin Linxiang; Kim Jaewook; Shin Yeon Kyun^*

来源：Biochemical Journal, 2016, 473(14): 2219-2224.

DOI：10.1042/BCJ20160339

• complexin
• fluorescence/Forster resonance energy transfer (FRET)
• nanodisc
• single molecule
• soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE)

Complexin (Cpx) is thought to be a major regulator of soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE)-dependent membrane fusion. Although the inhibition of membrane fusion by Cpx has been frequently reported, its structural basis has been elusive and an anticipated disruption of the SNARE core has never been observed. In the present study, to mimic the natural environment, we assembled a single SNAREpin between two nanodisc membrane patches. Single-molecule FRET (smFRET) detects a large conformational change, specifically at the C-terminal half, whereas no conformational change is observed at the N-terminal half. Our results suggest that Cpx splits the C-terminal half of the SNARE core at least 10 angstrom (1 angstrom=0.1 nm), whereby inhibiting further progression of SNARE zippering and membrane fusion.

• 出版日期2016-7