|
type |
Journal Article |
authors |
Grote, E.; Vlacich, G.; Pypaert, M.; Novick, P. J. |
title |
A snc1 endocytosis mutant: phenotypic analysis and suppression by overproduction of dihydrosphingosine phosphate lyase |
journal |
Mol Biol Cell |
Activity |
4.1.2.27 |
ui |
20556001 |
year |
(2000) |
volume |
11 |
number |
12 |
pages |
4051-65. |
| |
keywords |
Aldehyde-Lyases/genetics/*physiology |
abstract |
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. |
last changed |
2002/11/12 16:17 |
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