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  The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.

Demircioglu, F. E., Burkhardt, P., & Fasshauer, D. (2014). The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex. Proceedings of the National Academy of Sciences of the United States of America, 111(38), 13828-13833. doi:10.1073/pnas.1408254111.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-F615-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-80ED-D
Genre: Journal Article

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 Creators:
Demircioglu, F. E.1, Author              
Burkhardt, P.2, Author              
Fasshauer, D.2, Author              
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578596              

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Free keywords: membrane fusion; ER-Golgi trafficking; protein-protein interaction; isothermal titration calorimetry; fluorescence spectroscopy
 Abstract: Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mode of action has proved challenging. SM proteins are thought to act primarily through one type of SNARE protein, the syntaxins. Despite high structural similarity, however, contrasting binding modes have been found for different SM proteins and syntaxins. Whereas the secretory SM protein Munc18 binds to the. closed conformation" of syntaxin 1, the ER-Golgi SM protein Sly1 interacts only with the N-peptide of Sed5. Recent findings, however, indicate that SM proteins might interact simultaneously with both syntaxin regions. In search for a common mechanism, we now reinvestigated the Sly1/Sed5 interaction. We found that individual Sed5 adopts a tight closed conformation. Sly1 binds to both the closed conformation and the N-peptide of Sed5, suggesting that this is the original binding mode of SM proteins and syntaxins. In contrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conformation of Sed5.

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Language(s): eng - English
 Dates: 2014-09-23
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1408254111
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 111 (38) Sequence Number: - Start / End Page: 13828 - 13833 Identifier: -