Complexin arrests a pool of docked vesicles for fast Ca2+ -dependent release
Regulated exocytosis requires that the assembly of the basic membrane fusion machinery is temporarily arrested. Synchronized membrane fusion is then caused by a specific trigger—a local rise of the Ca2+ concentration. Using reconstituted giant unilamellar vesicles (GUVs), we have analysed the role o...
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| Hauptverfasser: | , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
15. June 2012
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| In: |
The EMBO journal
Year: 2012, Jahrgang: 31, Heft: 15, Pages: 3270-3281 |
| ISSN: | 1460-2075 |
| DOI: | 10.1038/emboj.2012.164 |
| Online-Zugang: | Verlag, Volltext: http://dx.doi.org/10.1038/emboj.2012.164 Verlag, Volltext: http://emboj.embopress.org/content/31/15/3270 
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| Verfasserangaben: | Jörg Malsam, Daniel Parisotto, Tanmay A. M. Bharat, Andrea Scheutzow, Jean Michel Krause, John A. G. Briggs and Thomas H. Söllner |
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| 520 | |a Regulated exocytosis requires that the assembly of the basic membrane fusion machinery is temporarily arrested. Synchronized membrane fusion is then caused by a specific trigger—a local rise of the Ca2+ concentration. Using reconstituted giant unilamellar vesicles (GUVs), we have analysed the role of complexin and membrane‐anchored synaptotagmin 1 in arresting and synchronizing fusion by lipid‐mixing and cryo‐electron microscopy. We find that they mediate the formation and consumption of docked small unilamellar vesicles (SUVs) via the following sequence of events: Synaptotagmin 1 mediates v‐SNARE‐SUV docking to t‐SNARE‐GUVs in a Ca2+‐independent manner. Complexin blocks vesicle consumption, causing accumulation of docked vesicles. Together with synaptotagmin 1, complexin synchronizes and stimulates rapid fusion of accumulated docked vesicles in response to physiological Ca2+ concentrations. Thus, the reconstituted assay resolves both the stimulatory and inhibitory function of complexin and mimics key aspects of synaptic vesicle fusion. | ||
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