title: A cascade of multiple proteins and lipids catalyzes membrane fusion.
abstract: Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly intotrans-complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fusion triggers such as Sec 17/α-SNAP and/or synaptotagmin, which insert their apolar "wedge" domains into the bilayers, initiating the lipid rearrangements of fusion.
authors.affiliation: Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH 03755 Bill.Wickner@Dartmouth.edu) Jose.Rizo-Rey@UTSouthwestern.edu.
authors.forename: William
authors.initials: W
authors.lastname: Wickner
authors.affiliation: Departments of Biophysics, Biochemistry, and Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390 Bill.Wickner@Dartmouth.edu) Jose.Rizo-Rey@UTSouthwestern.edu.
authors.forename: Josep
authors.initials: J
authors.lastname: Rizo
mesh_terms: D000818:Animals; D006801:Humans; D008055:Lipids; D008561:Membrane Fusion / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism; D051938:Munc18 Proteins / Q000378:metabolism / Q000502:physiology; D011485:Protein Binding; D050600:SNARE Proteins / Q000378:metabolism* / Q000502:physiology*; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
chemical_list: D008055:Lipids; D008565:Membrane Proteins; D051938:Munc18 Proteins; D050600:SNARE Proteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins