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Vol. 11, Issue 12, 4051-4065, December 2000
Department of Cell Biology, Yale University School of Medicine, New
Haven, Connecticut 06520-8002
The v-SNARE proteins Snc1p and Snc2p are required for fusion of
secretory vesicles with the plasma membrane in yeast. Mutation of a
methionine-based sorting signal in the cytoplasmic domain of either
Sncp inhibits Sncp endocytosis and prevents recycling of Sncp to the
Golgi after exocytosis. snc1-M43A mutant yeast have
reduced growth and secretion rates and accumulate post-Golgi secretory
vesicles and fragmented vacuoles. However, cells continue to grow and
secrete for several hours after de novo Snc2-M42A synthesis is
repressed. DPL1, the structural gene for
dihydrosphingosine phosphate lyase, was selected as a high copy number
snc1-M43A suppressor. Because DPL1 also
partially suppresses the growth and secretion phenotypes of a
snc deletion, we propose that enhanced degradation of
dihydrosphingosine-1-phosphate allows an alternative protein to replace
Sncp as the secretory vesicle v-SNARE.
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