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.
","abstract_html":"<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>","abstract_has_math":false,"creators":["Hayden, Jacob Robert"],"institution":null,"degree_name":"Master of Science in Biology","degree_level":"Masters","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Kyoungtae Kim"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012-01-01T08:00:00Z","date_published":"2012-01-01T08:00:00Z","updated_at":"2026-07-24T03:16:17Z","subjects":["Vps1","endosome","vacuole","trafficking","FM4-64","Biology"],"languages":[],"rights":["© Jacob Robert Hayden"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://bearworks.missouristate.edu/theses/1298","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kyoungtae Kim"]},{"key":"dc:creator","label":"Author","values":["Hayden, Jacob Robert"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Biology"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Vps1","endosome","vacuole","trafficking","FM4-64","Biology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© Jacob Robert Hayden"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://bearworks.missouristate.edu/theses/1298"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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.
"]},{"key":"dc:title","label":"Title","values":["Vps1's Implication on Late Endosome-to-Vacuole Traffic"]}]}],"canonical_facts":{"dc:contributor":["Kyoungtae Kim"],"dc:creator":["Hayden, Jacob Robert"],"dc:description.abstract":["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.
"],"dc:identifier":["https://bearworks.missouristate.edu/theses/1298"],"dc:rights":["© Jacob Robert Hayden"],"dc:subject":["Vps1","endosome","vacuole","trafficking","FM4-64","Biology"],"dc:title":["Vps1's Implication on Late Endosome-to-Vacuole Traffic"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science in Biology"]},"updated_at":"2026-07-24T03:16:17Z"}