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TitleNSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateJul 9, 2018
AuthorsUcheor B Choi / Minglei Zhao / K Ian White / Richard A Pfuetzner / Luis Esquivies / Qiangjun Zhou / Axel T Brunger /
PubMed AbstractSNARE complex disassembly by the ATPase NSF is essential for neurotransmitter release and other membrane trafficking processes. We developed a single-molecule FRET assay to monitor repeated rounds of ...SNARE complex disassembly by the ATPase NSF is essential for neurotransmitter release and other membrane trafficking processes. We developed a single-molecule FRET assay to monitor repeated rounds of NSF-mediated disassembly and reassembly of individual SNARE complexes. For ternary neuronal SNARE complexes, disassembly proceeds in a single step within 100 msec. We observed short- (<0.32 s) and long-lived (≥0.32 s) disassembled states. The long-lived states represent fully disassembled SNARE complex, while the short-lived states correspond to failed disassembly or immediate reassembly. Either high ionic strength or decreased αSNAP concentration reduces the disassembly rate while increasing the frequency of short-lived states. NSF is also capable of disassembling anti-parallel ternary SNARE complexes, implicating it in quality control. Finally, complexin-1 competes with αSNAP binding to the SNARE complex; addition of complexin-1 has an effect similar to that of decreasing the αSNAP concentration, possibly differentially regulating cis and trans SNARE complexes disassembly.
External linksElife / PubMed:29985126 / PubMed Central
MethodsEM (single particle)
Resolution7.0 Å
Structure data

EMDB-8944:
20S supercomplex consisting of linked neuronal SNARE complex, alpha-SNAP, and N-ethylmaleimide sensitive factor (NSF)
Method: EM (single particle) / Resolution: 7.0 Å

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