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

Gallwitz, D.; Jahn, R.

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

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Gallwitz, D.
Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society;

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Jahn, R.
Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society;

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Citation

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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F158-B

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.