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Ordering the final events in yeast exocytosis.

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, 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.

Pubmed ID: 11038189


  • Grote E
  • Carr CM
  • Novick PJ


The Journal of cell biology

Publication Data

October 16, 2000

Associated Grants


Mesh Terms

  • Adenosine Triphosphatases
  • Carrier Proteins
  • Cell Membrane
  • Cell Polarity
  • Exocytosis
  • Fungal Proteins
  • GTP-Binding Proteins
  • Guanine Nucleotide Exchange Factors
  • Membrane Fusion
  • Membrane Proteins
  • Models, Biological
  • Munc18 Proteins
  • N-Ethylmaleimide-Sensitive Proteins
  • Nerve Tissue Proteins
  • Qa-SNARE Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae Proteins
  • Transport Vesicles
  • Vesicular Transport Proteins
  • Yeasts