Abstract
In yeast, assembly of exocytic soluble N-ethylmaleimide-sensitive 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, cisoSNARE complexes containing surface-accessible Sncp accumulate in the plasma membrane. Thus, one function of Sec18p is to disassemble SNARE complexes on the postfusion membrane.
Original language | English (US) |
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Pages (from-to) | 439-451 |
Number of pages | 13 |
Journal | Journal of Cell Biology |
Volume | 151 |
Issue number | 2 |
DOIs | |
State | Published - Oct 16 2000 |
Externally published | Yes |
Keywords
- Exocyst
- Membrane fusion
- NSF
- SNAREs
- Sec1
ASJC Scopus subject areas
- Cell Biology