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Ordering the final events in yeast exocytosis.

http://www.ncbi.nlm.nih.gov/pubmed/11038189

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 RIS Download

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

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