SNAREpin Assembly by Munc18-1 Requires Previous Vesicle Docking by Synaptotagmin 1
Regulated exocytosis requires the general membrane fusion machinery-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins. Using reconstituted giant unilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1·SNAP-25), we determined...
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| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2012
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| In: |
The journal of biological chemistry
Year: 2012, Jahrgang: 287, Heft: 37, Pages: 31041-31049 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M112.386805 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1074/jbc.M112.386805 Verlag, kostenfrei, Volltext: http://www.jbc.org/content/287/37/31041 
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| Verfasserangaben: | Daniel Parisotto, Jörg Malsam, Andrea Scheutzow, Jean Michel Krause, Thomas H. Söllner |
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| 245 | 1 | 0 | |a SNAREpin Assembly by Munc18-1 Requires Previous Vesicle Docking by Synaptotagmin 1 |c Daniel Parisotto, Jörg Malsam, Andrea Scheutzow, Jean Michel Krause, Thomas H. Söllner |
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| 520 | |a Regulated exocytosis requires the general membrane fusion machinery-soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins. Using reconstituted giant unilamellar vesicles containing preassembled t-SNARE proteins (syntaxin 1·SNAP-25), we determined how Munc18-1 controls the docking, priming, and fusion of small unilamellar vesicles containing the v-SNARE VAMP2 and the Ca2+ sensor synaptotagmin 1. In vitro assays allowed us to position Munc18-1 in the center of a sequential reaction cascade; vesicle docking by synaptotagmin 1 is a prerequisite for Munc18-1 to accelerate trans-SNARE complex (SNAREpin) assembly and membrane fusion. Complexin II stalls SNAREpin zippering at a late stage and, hence, contributes to synchronize membrane fusion in a Ca2+- and synaptotagmin 1-dependent manner. Thus, at the neuronal synapse, the priming factor Munc18-1 may accelerate the conversion of docked synaptic vesicles into a readily releasable pool by activating SNAREs for efficient membrane fusion. | ||
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