Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13
| Autor: | Le Zhu, Cong Ma, Tianzhi Li, Yun Li, Shen Wang |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Vesicle fusion Synaptosomal-Associated Protein 25 Vesicle-Associated Membrane Protein 2 SNARE binding Chemistry Biophysics Syntaxin 1 Lipid bilayer fusion Nerve Tissue Proteins Cell Biology Biochemistry Exocytosis Cell biology R-SNARE Proteins 03 medical and health sciences Munc18 Proteins 030104 developmental biology Structural Biology Multiprotein Complexes Genetics Humans SNARE complex Molecular Biology SNARE complex assembly |
| Zdroj: | FEBS Letters. 592:1161-1172 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.13018 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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