title: Molecular form follows function: (un)snaring the SNAREs.
abstract: Exocytotic release of transmitters is mediated by the ternary SNARE complex. The form of this complex is consistent with its function in the positioning of vesicles to the plasma membrane and their fusion to it. Recent advances in single-molecule techniques, however, bring an additional layer of complexity to this process, implicating that there might be various modes of operation. For example, the binary syntaxin-synaptobrevin 2 complex, in addition to the ternary complex containing SNAP25, might enable vesicular docking. Single-molecule techniques allow direct measurements of the distance/extension, rupture force, spontaneous dissociation times and interaction energy for SNARE protein-protein interactions. These measurements are complementary to results and conclusions drawn from other techniques. Consequently, single-molecule techniques promise tremendous opportunities for in vitro investigations of SNARE proteins to improve our understanding of their role in exocytosis.
authors.affiliation: Department of Neurobiology, Civitan International Research Center, Evelyn F. McKnight Brain Institute, Atomic Force Microscopy and Nanotechnology Laboratories, University of Alabama, Birmingham, AL 35294, USA. vlad@uab.edu
authors.forename: Vladimir
authors.initials: V
authors.lastname: Parpura
authors.forename: U
authors.initials: U
authors.lastname: Mohideen
mesh_terms: D000818:Animals; D005089:Exocytosis / Q000502:physiology*; D006801:Humans; D011487:Protein Conformation; D050600:SNARE Proteins / Q000737:chemistry / Q000502:physiology*; D013329:Structure-Activity Relationship; D013572:Synaptic Vesicles / Q000502:physiology
chemical_list: D050600:SNARE Proteins