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          Institute: MPI für experimentelle Medizin     Collection: Molecular Neurobiology     Display Documents

ID: 292217.0, MPI für experimentelle Medizin / Molecular Neurobiology
Identification of the minimal protein domain required for priming activity of Munc13-1
Authors:Stevens, David R.; Wu, Zheng-Xing; Matti, Ulf; Junge, Harald J.; Schirra, Claudia; Becherer, Ute; Wojcik, Sonja M.; Brose, Nils; Rettig, Jens
Date of Publication (YYYY-MM-DD):2005-12
Title of Journal:Current Biology
Issue / Number:24
Start Page:2243
End Page:2248
Review Status:Peer-review
Audience:Experts Only
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Communicated by:Nils Brose
Affiliations:MPI für experimentelle Medizin/Molecular neurobiology
Relations:Has References-DOI:10.1016/j.cub.2005.10.055
Identifiers:ISSN:0960-9822 [ID No:1]
ISI:000234330300023 [ID No:2]
ISI:000234330300023 [ID No:3]
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