Energetics and dynamics of SNAREpin folding across lipid bilayers
- 30 September 2007
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Structural & Molecular Biology
- Vol. 14 (10), 890-896
- https://doi.org/10.1038/nsmb1310
Abstract
Membrane fusion occurs when SNAREpins fold up between lipid bilayers. How much energy is generated during SNAREpin folding and how this energy is coupled to the fusion of apposing membranes is unknown. We have used a surface forces apparatus to determine the energetics and dynamics of SNAREpin formation and characterize the different intermediate structures sampled by cognate SNAREs in the course of their assembly. The interaction energy–versus–distance profiles of assembling SNAREpins reveal that SNARE motifs begin to interact when the membranes are 8 nm apart. Even after very close approach of the bilayers ( ∼ 2–4 nm), the SNAREpins remain partly unstructured in their membrane-proximal region. The energy stabilizing a single SNAREpin in this configuration (35 kBT) corresponds closely with the energy needed to fuse outer but not inner leaflets (hemifusion) of pure lipid bilayers (40–50 kBT).This publication has 60 references indexed in Scilit:
- FUSION PORES AND FUSION MACHINES IN CA2+-TRIGGERED EXOCYTOSISAnnual Review of Biophysics and Biophysical Chemistry, 2006
- Structure and function of SNARE and SNARE-interacting proteinsQuarterly Reviews of Biophysics, 2005
- The Energetics of Membrane Fusion from Binding, through Hemifusion, Pore Formation, and Pore EnlargementThe Journal of Membrane Biology, 2004
- Membrane fusion: a structural perspective on the interplay of lipids and proteinsCurrent Opinion in Structural Biology, 2003
- Fusion of Cells by Flipped SNAREsScience, 2003
- Protein-Lipid Interplay in Fusion and Fission of Biological MembranesAnnual Review of Biochemistry, 2003
- SNAREpins: Minimal Machinery for Membrane FusionCell, 1998
- Structural Changes Are Associated with Soluble N-Ethylmaleimide-sensitive Fusion Protein Attachment Protein Receptor Complex FormationJournal of Biological Chemistry, 1997
- A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusionCell, 1993
- SNAP receptors implicated in vesicle targeting and fusionNature, 1993