Assembly and disassembly of the SNARE membrane-protein complexes plays a key role in vesicular trafficking. The SM-family Sly1 protein binds to the tSNARE Sed5 protein and stimulates its assembly into a trans-SNARE complex. Disassembly of the resulting cis-SNARE complex containing Sed5 was retarded in a temperature-sensitive yeast mutant of Sly1 protein with a defect in binding to Sed5. A temperature-sensitive mutation (sec18-1) of Sec18/NSF disassembly ATPase showed synthetic lethality with the sly1^ts mutation. These results suggest that Sly1 and Sec18 proteins work cooperatively and that the binding of Sly1 to Sed5 stimulates the disassembly of the cis-SNARE complex by Sec18 ATPase.

This article cannot obtain the latest cited-by information.