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The ionic layer is required for efficient dissociation of the SNARE complex by a-SNAP and NSF



The ionic layer is required for efficient dissociation of the SNARE complex by a-SNAP and NSF



Proceedings of the National Academy of Sciences of the United States of America 98(25): 262-7



The ionic-layer glutamine of syntaxin is necessary for efficient a-SNAP (a-soluble N-ethylmalemide-sensitive fusion protein (NSF) attachment protein) and NSF-mediated dissociation of the complex. This layer is part of the soluble NSF attachment protein receptor (SNARE) complex that mediates intracellular membrane fusion. When the glutamine residue is mutated, the SNARE complex still bound to a-SNAP and NSF and was released through ATP hydrolysis by NSF. However, the complex no longer dissociated into SNARE monomers. These results suggest that a-SNAP and NSF drive conformational changes at the ionic layer via specific interactions with the syntaxin glutamine, leading to the dissociation of the SNARE complex.

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