title: How could SNARE proteins open a fusion pore?
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.
authors.affiliation: 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.
authors.forename: Qinghua
authors.initials: Q
authors.lastname: Fang
authors.affiliation: 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.
authors.forename: Manfred
authors.initials: M
authors.lastname: Lindau
mesh_terms: D000818:Animals; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D009490:Neurosecretory Systems / Q000502:physiology; D011487:Protein Conformation; D050600:SNARE Proteins / Q000737:chemistry / Q000502:physiology*; D013572:Synaptic Vesicles / Q000502:physiology*
chemical_list: D050600:SNARE Proteins