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Physiology (Bethesda). 2014 Jul;29(4):278-85. doi: 10.1152/physiol.00026.2013.

How could SNARE proteins open a fusion pore?

Author information

1
School of Applied and Engineering Physics, Cornell University, Ithaca, New York; and Laboratory for Nanoscale Cell Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany.
2
School of Applied and Engineering Physics, Cornell University, Ithaca, New York; and Laboratory for Nanoscale Cell Biology, Max-Planck-Institute for Biophysical Chemistry, Göttingen, Germany ml95@cornell.edu.

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.

PMID:
24985331
PMCID:
PMC4103061
DOI:
10.1152/physiol.00026.2013
[Indexed for MEDLINE]
Free PMC Article

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