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  The riddle of the Sec1/Munc-18 proteins - new twists added to their interactions with SNAREs

Gallwitz, D., & Jahn, R. (2003). The riddle of the Sec1/Munc-18 proteins - new twists added to their interactions with SNAREs. Trends in Biochemical Sciences, 28(3), 113-116. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6TCV-47WD8KK-2-3&_cdi=5180&_user=38661&_pii=S0968000403000288&_orig=search&_coverDate=03%2F31%2F2003&_sk=999719996&view=c&wchp=dGLzVtz-zSkWb&md5=a9086719b9b6d60a21af212285864623&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F158-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E41E-6
Genre: Journal Article

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20754.pdf (Publisher version), 0B
 
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 Creators:
Gallwitz, D.1, Author              
Jahn, R.2, Author              
Affiliations:
1Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622              
2Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              

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 Abstract: Sec1/Munc-18 (SM) proteins are essential for intracellular membrane fusion reactions. Most of them bind to membrane- associated soluble N-ethylmaleimide-sensitive fusion (NSF)- attachment protein receptors (SNAREs) of the syntaxin subfamily but it is unclear whether regulating syntaxins is their primary role. Recent studies now have shown that the mechanism of syntaxin binding is not conserved, even though the structures of both protein families are. Amazing as this might be for those considering the evolution of conserved folds, it leaves the question of how SM proteins operate in membrane fusion unanswered.

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Language(s): eng - English
 Dates: 2003-03
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Trends in Biochemical Sciences
Source Genre: Journal
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Pages: - Volume / Issue: 28 (3) Sequence Number: - Start / End Page: 113 - 116 Identifier: -