Abstract
dc:description.abstract<p>Previous studies have shown Vps1 to be necessary for both sorting of soluble vacuolar proteins from the Golgi and retention of Golgi membrane proteins. I have recently found that Vps1 is implicated in membrane trafficking from the plasma membrane through the endosomal system to the vacuole. Loss of Vps1 resulted in accumulation of FM4-64 puncta that colocalize with a late endosomal marker (GFP-Pep12), indicating a slower late endosome-to-vacuole traffic. In addition, Vps1 was found to genetically interact with Vps36 and Ypt7, which are involved in the late endosome-to-vacuole traffic. Protein's functional role is generally correlated with its localization, so I investigated the subcellular localization of Vps1-GFP in relation to endocytic sites and endosomal compartments. In a FM4-64 pulse-chase experiment, I found that the extent of colocalization of FM4-64 with Vps1-GFP drastically increased after 20 min chase, indicating Vps1-carrying vesicles are among the population of late endosomal compartments. Consistently, I observed that Vps1-GFP coincides with PI3P (endosomal marker), but not with the plasma membrane endocytic markers such as Abp1 and Ede1, suggesting that Vps1 is a component of endosomal compartments. Taken together, I postulate that Vps1 is required for an efficient traffic toward the vacuole from late endosomal compartments.</p>
Degree
thesis:*- Name thesis:degree_name
- Master of Science in Biology
- Level thesis:degree_level
- Masters
- Discipline thesis:degree_discipline
- Biology
- Year
- 2012
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Hayden, Jacob Robert
- Contributors dc:contributor
-
- Kyoungtae Kim
Subjects
dc:subject × 6Rights
dc:rights- Statement dc:rights
-
- © Jacob Robert Hayden
Identifiers
dc:identifier.*- Repository record dc:identifier
- https://bearworks.missouristate.edu/theses/1298
- OAI identifier oai:identifier
- oai:bearworks.missouristate.edu:theses-2299