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  How could SNARE proteins open a fusion pore?

Fang, Q., & Lindau, M. (2014). How could SNARE proteins open a fusion pore? Physiology, 29(4), 278-285. doi:10.1152/physiol.00026.2013.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0019-FEC0-3 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-110F-9
Genre: Journal Article

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2043838.pdf (Publisher version), 2MB
 
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 Creators:
Fang, Q.1, Author           
Lindau, M.1, Author           
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1Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1832294              

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 Abstract: The SNARE (Soluble NSF Attachment protein REceptor) complex, which in mammalian neurosecretory cells is composed of the proteins synaptobrevin 2 (also called VAMP2), syntaxin, and SNAP-25, plays a key role in vesicle fusion. In this review, we discuss the hypothesis that, in neurosecretory cells, fusion pore formation is directly accomplished by a conformational change in the SNARE complex via movement of the transmembrane domains.

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Language(s): eng - English
 Dates: 2014-07-01
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: DOI: 10.1152/physiol.00026.2013
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Title: Physiology
Source Genre: Journal
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Pages: - Volume / Issue: 29 (4) Sequence Number: - Start / End Page: 278 - 285 Identifier: -