Identifying novel interaction partners of the exocyst member Sec8 in the fission yeast Schizosaccharomyces pombe
Adams, Lauren
Date: 22 September 2017
Publisher
University of Exeter
Degree Title
MbyRes Biological Sciences
Abstract
The exocyst is a complex of proteins classically known for its role in tethering secretory vesicles during exocytosis, but it has since been shown to participate in a whole host of other cellular processes. Several human patients have been discovered in whom mutations in the exocyst appear to cause disease, but the underlying mechanisms ...
The exocyst is a complex of proteins classically known for its role in tethering secretory vesicles during exocytosis, but it has since been shown to participate in a whole host of other cellular processes. Several human patients have been discovered in whom mutations in the exocyst appear to cause disease, but the underlying mechanisms are still poorly understood. This highlights an urgent need to better characterise these proteins. The exocyst complex is conserved in the fission yeast Schizosaccharomyces pombe, which is an ideal model eukaryote in which to examine conserved biological mechanisms. In this study, I used GFP-Trap combined with qualitative proteomics to reassess the role of exocyst component Sec8. Unexpectedly, this uncovered putative novel associations with both the nuclear envelope and the mitochondrial envelope. Using live-cell imaging, I further showed that cells expressing mutated Sec8 displayed altered mitochondrial morphology and a significant reduction in mitochondrial fusion. This indicates that Sec8 is somehow involved in mitochondrial distribution and dynamics, a role which has not been previously described. This may provide further insight into the role of the exocyst in both normal and pathological conditions.
MbyRes Dissertations
Doctoral College
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