Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 7, Pages 700-706Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1433
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Funding
- NIGMS NIH HHS [R01 GM067629, R01 GM067629-03, R01 GM051290, R01 GM067629-02, R01 GM067629-04, R01 GM067629-05, R01 GM067629-01] Funding Source: Medline
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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.
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