Journal
JOURNAL OF CELL BIOLOGY
Volume 148, Issue 6, Pages 1231-1238Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.148.6.1231
Keywords
Vps39/Vam6p; Vps41/Vam2p; Ypt7p; priming; Rab/Ypt effector
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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 effecters, and these effecters can be mobilized by NSF/Sec18p-driven priming, allowing their direct association with a Rab/Ypt protein to activate docking.
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