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, 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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases*
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Carrier Proteins / metabolism
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Cell Membrane / metabolism
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Cell Polarity
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Exocytosis*
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Fungal Proteins / metabolism*
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GTP-Binding Proteins / metabolism
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Guanine Nucleotide Exchange Factors
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Membrane Fusion*
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Membrane Proteins / metabolism*
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Models, Biological
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Munc18 Proteins
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N-Ethylmaleimide-Sensitive Proteins
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Nerve Tissue Proteins / metabolism
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Qa-SNARE Proteins
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R-SNARE Proteins
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SNARE Proteins
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Saccharomyces cerevisiae Proteins*
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Transport Vesicles / metabolism
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Vesicular Transport Proteins*
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Yeasts
Substances
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Carrier Proteins
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Fungal Proteins
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Guanine Nucleotide Exchange Factors
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Membrane Proteins
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Munc18 Proteins
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Nerve Tissue Proteins
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Qa-SNARE Proteins
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R-SNARE Proteins
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SEC2 protein, S cerevisiae
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SNARE Proteins
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SNC1 protein, S cerevisiae
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SNC2 protein, S cerevisiae
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SSO1 protein, S cerevisiae
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SSO2 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Vesicular Transport Proteins
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Adenosine Triphosphatases
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GTP-Binding Proteins
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SEC18 protein, S cerevisiae
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N-Ethylmaleimide-Sensitive Proteins