The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein.
The homotypic fusion of yeast vacuoles requires Sec18p (NSF)-driven priming to allow vacuole docking, but the mechanism that links priming and docking is unknown. We find that a large multisubunit protein called the Vam2/6p complex is bound to cis-paired SNAP receptors (SNAREs) on isolated vacuoles. This association of the Vam2/6p ... complex with the cis-SNARE complex is disrupted during priming. The Vam2/6p complex then binds to Ypt7p, a guanosine triphosphate binding protein of the Rab family, to initiate productive contact between vacuoles. Thus, cis-SNARE complexes can contain Rab/Ypt effectors, and these effectors can be mobilized by NSF/Sec18p-driven priming, allowing their direct association with a Rab/Ypt protein to activate docking.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Adenosine Triphosphatases, Carrier Proteins, Fungal Proteins, Membrane Fusion, Membrane Proteins, Models, Biological, Nuclear Proteins, RNA-Binding Proteins, SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles, Vesicular Transport Proteins, rab GTP-Binding Proteins
Adaptor Proteins, Vesicular Transport, Adenosine Triphosphatases, Carrier Proteins, Fungal Proteins, Membrane Fusion, Membrane Proteins, Models, Biological, Nuclear Proteins, RNA-Binding Proteins, SNARE Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles, Vesicular Transport Proteins, rab GTP-Binding Proteins
J. Cell Biol.
Date: Mar. 20, 2000
PubMed ID: 10725336
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