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Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13
Author(s) -
Li Yun,
Wang Shen,
Li Tianzhi,
Zhu Le,
Ma Cong
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13018
Subject(s) - snare complex , synaptobrevin , exocytosis , syntaxin , lipid bilayer fusion , microbiology and biotechnology , chemistry , biology , synaptic vesicle , biochemistry , vesicle , secretion , membrane
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.