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How could SNARE proteins open a fusion pore?

MPS-Authors
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Fang,  Q.
Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Lindau,  M.
Research Group of Nanoscale Cell Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

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


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-FEC0-3
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.