Article abstract
Nature Structural & Molecular Biology 15, 700 - 706 (2008)
Published online: 15 June 2008 | doi:10.1038/nsmb.1433
Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion
Xiaobing Lu1,2, Yinghui Zhang1,2 & Yeon-Kyun Shin1
Abstract
Formation of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex facilitates intracellular membrane fusion. A single SNARE complex is thought to be insufficient; multiple copies of SNARE complexes must work cooperatively. However, the mechanism by which such a higher-order SNARE protein structure is assembled is unknown. EPR and fluorescence analyses show that at least three copies of target-membrane SNARE proteins self-assemble through the interaction between the transmembrane domains (TMDs), and this multimeric structure serves as scaffolding for trans-SNARE assembly. SNARE core formation in solution induces oligomerization of the TMDs of vesicle-associated SNAREs in the apposing membrane, transiently forming a supramolecular protein structure spanning two membranes. This higher-order protein intermediate evolves, by involving lipid molecules, to the hemifusion state. Hemifusion is subsequently followed by distal leaflet mixing and formation of the cis-SNARE complex.
- Department of Biochemistry, Biophysics and Molecular Biology, Molecular Biology Building, Iowa State University, Ames, Iowa 50011, USA.
- These authors contributed equally to this work.
Correspondence to: Yeon-Kyun Shin1 e-mail: colishin@iastate.edu
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