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Identification of the minimal protein domain required for priming activity of Munc13-1

MPG-Autoren
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Junge,  Harald J.
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Becherer,  Ute
Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Wojcik,  Sonja M.
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Brose,  Nils
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Zitation

Stevens, D. R., Wu, Z.-X., Matti, U., Junge, H. J., Schirra, C., Becherer, U., et al. (2005). Identification of the minimal protein domain required for priming activity of Munc13-1. Current Biology, 15(24), 2243-2248. doi:10.1016/j.cub.2005.10.055.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-002A-1EE2-0
Zusammenfassung
Most nerve cells communicate with each other through synaptic transmission at chemical synapses. The regulated exocytosis of neurotransmitters, hormones, and peptides occurs at specialized membrane areas through Ca2+-triggered fusion of secretory vesicles with the plasma membrane [1-7]. Prior to fusion, vesicles are docked at the plasma membrane and must then be rendered fusion-competent through a process called priming. The molecular mechanism underlying this priming process is most likely the formation of the SNARE complex consisting of Syntaxin 1, SNAP-25, and Synaptobrevin 2. Members of the Munc13 protein family consisting of Munc13-1, -2, -3, and -4 were found to be absolutely required for this priming process [8-13]. In the present study, we identified the minimal Munc13-1 domain that is responsible for its priming activity. Using Munc13-1 deletion constructs in an electrophysiological gain-of-function assay of chromaffin-granule secretion, we show that priming activity is mediated by the C-terminal residues 1100-1735 of Munc13-1, which contains both Munc13-homology domains and the C-terminal C-2 domain. Priming by Munc13-1 appears to require its interaction with Syntaxin 1 because point mutants that do not bind Syntaxin 1 do not prime chrornaffin granules.