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

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.

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 Creators:
Stevens, David R., Author
Wu, Zheng-Xing, Author
Matti, Ulf, Author
Junge, Harald J.1, Author              
Schirra, Claudia, Author
Becherer, Ute2, Author              
Wojcik, Sonja M.1, Author              
Brose, Nils1, Author              
Rettig, Jens, Author
Affiliations:
1Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173659              
2Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173656              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2005-12
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 292217
ISI: 000234330300023
ISI: 000234330300023
DOI: 10.1016/j.cub.2005.10.055
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Title: Current Biology
Source Genre: Journal
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Pages: - Volume / Issue: 15 (24) Sequence Number: - Start / End Page: 2243 - 2248 Identifier: ISSN: 0960-9822