title: Tethering the assembly of SNARE complexes.
abstract: The fusion of transport vesicles with their target membranes is fundamental for intracellular membrane trafficking and diverse physiological processes and is driven by the assembly of functional soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes. Prior to fusion, transport vesicles are physically linked to their target membranes by various tethering factors. Recent studies suggest that tethering factors also positively regulate the assembly of functional SNARE complexes, thereby coupling tethering with fusion events. This coupling is mediated, at least in part, by direct physical interactions between tethering factors, SNAREs, and Sec1/Munc18 (SM) proteins. In this review we summarize recent progress in understanding the roles of tethering factors in the assembly of specific and functional SNARE complexes driving membrane-fusion events.
authors.affiliation: School of Pharmaceutical Sciences, Xiamen University, Xiamen, People's Republic of China; Institute of Molecular and Cell Biology, Singapore.
authors.forename: WanJin
authors.initials: W
authors.lastname: Hong
authors.affiliation: Molecular Cell Biology Department, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: Sima.Lev@weizmann.ac.il.
authors.forename: Sima
authors.initials: S
authors.lastname: Lev
mesh_terms: D000818:Animals; D006801:Humans; D008561:Membrane Fusion; D046912:Multiprotein Complexes / Q000378:metabolism; D055503:Protein Multimerization; D021122:Protein Subunits / Q000378:metabolism; D021381:Protein Transport; D050600:SNARE Proteins / Q000378:metabolism*; D022161:Transport Vesicles / Q000378:metabolism; D033921:Vesicular Transport Proteins / Q000378:metabolism
chemical_list: D046912:Multiprotein Complexes; D021122:Protein Subunits; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins
keywords: SM proteins; SNAREpin; SNAREs; membrane fusion; tethering factors