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Original Article |
Correspondence to: Peter J. Novick, Dept. Cell Biology, Yale University School of Medicine, 333 Cedar St., New Haven, CT 06520-8002. Tel:(203) 785-5871 Fax:(203) 785-7226
In yeast, assembly of exocytic soluble N-ethylmaleimidesensitive fusion protein (NSF) attachment protein receptor (SNARE) complexes between the secretory vesicle SNARE Sncp and the plasma membrane SNAREs Ssop and Sec9p occurs at a late stage of the exocytic reaction. Mutations that block either secretory vesicle delivery or tethering prevent SNARE complex assembly and the localization of Sec1p, a SNARE complex binding protein, to sites of secretion. By contrast, wild-type levels of SNARE complexes persist in the sec1-1 mutant after a secretory block is imposed, suggesting a role for Sec1p after SNARE complex assembly. In the sec18-1 mutant, cis-SNARE complexes containing surface-accessible Sncp accumulate in the plasma membrane. Thus, one function of Sec18p is to disassemble SNARE complexes on the postfusion membrane.
Key Words: NSF, membrane fusion, SNAREs, exocyst, Sec1
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