Journal
FEBS LETTERS
Volume 592, Issue 7, Pages 1161-1172Publisher
WILEY
DOI: 10.1002/1873-3468.13018
Keywords
membrane fusion; Munc13; SNARE complex assembly; synaptic exocytosis; tomosyn
Funding
- National Natural Science Foundation of China [31670846, 31322034, 31721002]
- National Key Basic Research Program of China [2015CB910800, 2014CB910203]
- Program for Changjiang Scholars and Innovative Research Team in University [PCSIRT: IRT13016]
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As a SNARE binding protein, tomosyn has been reported to negatively regulate synaptic exocytosis via arresting syntaxin-1 and SNAP-25 into a nonfusogenic product that precludes synaptobrevin-2 entry, raising the question how the assembly of the SNARE complex is achieved. Here, we have investigated new functions of tomosyn in SNARE complex formation and SNARE-mediated vesicle fusion. Assisted by NSF/alpha-SNAP, syntaxin-1 escapes tomosyn arrest and assembles into the Munc18-1/syntaxin-1 complex. Munc13-1 then catalyzes the transit of syntaxin-1 from the Munc18-1/syntaxin-1 complex to the SNARE complex in a manner specific to synaptobrevin-2 but resistant to tomosyn. Our data suggest that tomosyn ensures SNARE assembly in a way amenable to tight regulation by Munc18-1 and Munc13-1.
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