An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) complex assembly
Munc18-1, a SEC1/Munc18 protein and key regulatory protein in synaptic transmission, can either promote or inhibit SNARE complex assembly. Although the binary inhibitory interaction between Munc18-1 and closed syntaxin 1 is well described, the mechanism of how Munc18-1 stimulates membrane fusion rem...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
February 14, 2014
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| In: |
The journal of biological chemistry
Year: 2014, Volume: 289, Issue: 14, Pages: 9639-9650 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M113.514273 |
| Online Access: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M113.514273 Verlag, lizenzpflichtig, Volltext: http://www.jbc.org/content/289/14/9639 
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| Author Notes: | Daniel Parisotto, Maximilian Pfau, Andrea Scheutzow, Klemens Wild, Matthias P. Mayer, Jörg Malsam, Irmgard Sinning, and Thomas H. Söllner |
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| 245 | 1 | 3 | |a An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) complex assembly |c Daniel Parisotto, Maximilian Pfau, Andrea Scheutzow, Klemens Wild, Matthias P. Mayer, Jörg Malsam, Irmgard Sinning, and Thomas H. Söllner |
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| 520 | |a Munc18-1, a SEC1/Munc18 protein and key regulatory protein in synaptic transmission, can either promote or inhibit SNARE complex assembly. Although the binary inhibitory interaction between Munc18-1 and closed syntaxin 1 is well described, the mechanism of how Munc18-1 stimulates membrane fusion remains elusive. Using a reconstituted assay that resolves vesicle docking, priming, clamping, and fusion during synaptic exocytosis, we show that helix 12 in domain 3a of Munc18-1 stimulates SNAREpin assembly and membrane fusion. A single point mutation (L348R) within helix 12 selectively abolishes VAMP2 binding and the stimulatory function of Munc18-1 in membrane fusion. In contrast, targeting a natural switch site (P335A) at the start of helix 12, which can result in an extended α-helical conformation, further accelerates lipid-mixing. Together with structural modeling, the data suggest that helix 12 provides a folding template for VAMP2, accelerating SNAREpin assembly and membrane fusion. Analogous SEC1/Munc18-SNARE interactions at other transport steps may provide a general mechanism to drive lipid bilayer merger. At the neuronal synapse, Munc18-1 may convert docked synaptic vesicles into a readily releasable pool. | ||
| 650 | 4 | |a Exocytosis | |
| 650 | 4 | |a Membrane Fusion | |
| 650 | 4 | |a Membrane Reconstitution | |
| 650 | 4 | |a Membrane Trafficking | |
| 650 | 4 | |a SM Protein | |
| 650 | 4 | |a Snare Proteins | |
| 650 | 4 | |a Synaptic Vesicle | |
| 650 | 4 | |a VAMP2/Synaptobrevin | |
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