Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13

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Abstract

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/α-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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Li, Y., Wang, S., Li, T., Zhu, L., & Ma, C. (2018). Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13. FEBS Letters, 592(7), 1161–1172. https://doi.org/10.1002/1873-3468.13018

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