title: SNARE zippering.
abstract: SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly conserved set of membrane-associated proteins that mediate intracellular membrane fusion. Cognate SNAREs from two separate membranes zipper to facilitate membrane apposition and fusion. Though the stable post-fusion conformation of SNARE complex has been extensively studied with biochemical and biophysical means, the pathway of SNARE zippering has been elusive. In this review, we describe some recent progress in understanding the pathway of SNARE zippering. We particularly focus on the half-zippered intermediate, which is most likely to serve as the main point of regulation by the auxiliary factors.
authors.affiliation: Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A.
authors.forename: Xiaochu
authors.initials: X
authors.lastname: Lou
authors.affiliation: Roy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, U.S.A. colishin@iastate.edu.
authors.forename: Yeon-Kyun
authors.initials: YK
authors.lastname: Shin
mesh_terms: D000818:Animals; D006801:Humans; D008561:Membrane Fusion; D051938:Munc18 Proteins / Q000378:metabolism; D011487:Protein Conformation; D050600:SNARE Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction; D050863:Synaptotagmin I / Q000378:metabolism
chemical_list: D051938:Munc18 Proteins; D050600:SNARE Proteins; D050863:Synaptotagmin I
keywords: Munc18-1; SNARE; coiled coil; complexin; four-helix bundle; nanodisc; synaptotagmin 1