{"id":{"repo_id":"mo-state","oai_identifier":"oai:bearworks.missouristate.edu:theses-2313"},"canonical_url":"https://search.dev.ndltd.org/etd/mo-state/oai:bearworks.missouristate.edu:theses-2313","repository":{"repo_id":"mo-state","name":"Missouri State University","base_url":"https://bearworks.missouristate.edu/do/oai/"},"display":{"title":"Inactivation of Tor Proteins Affects the Dynamics of Endocytic Proteins in Early Stage of Endocytosis","abstract":"<p>Tor2 is an activator of the Rom2/Rho1 pathway that regulates α-factor internalization. Since the recruitment of endocytic proteins such as actin binding proteins and the amphiphysins precedes the internalization of α-factor, I hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. I report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants. Furthermore, I found that the endocytic proteins Rvs167 and Sjl2 are completely mistargeted to the cytoplasm in tor1∆tor2ts double mutant cells. I also demonstrate here that the efficiency of endocytic internalization or scission in all tor mutants was drastically decreased. In agreement with the Sjl2 mislocalization, I found that in tor1∆tor2ts double mutant cells, as well as other tor mutant cells, the overall PIP2 level was dramatically increased. Finally, the cell wall chitin content in tor2ts and tor1∆tor2ts mutant cells was also significantly increased. Taken together, both functional Tor proteins, Tor1 and Tor2, are essentially required for proper endocytic protein dynamics at the early stage of endocytosis.</p>","abstract_html":"&lt;p&gt;Tor2 is an activator of the Rom2/Rho1 pathway that regulates α-factor internalization. Since the recruitment of endocytic proteins such as actin binding proteins and the amphiphysins precedes the internalization of α-factor, I hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. I report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants. Furthermore, I found that the endocytic proteins Rvs167 and Sjl2 are completely mistargeted to the cytoplasm in tor1∆tor2ts double mutant cells. I also demonstrate here that the efficiency of endocytic internalization or scission in all tor mutants was drastically decreased. In agreement with the Sjl2 mislocalization, I found that in tor1∆tor2ts double mutant cells, as well as other tor mutant cells, the overall PIP2 level was dramatically increased. Finally, the cell wall chitin content in tor2ts and tor1∆tor2ts mutant cells was also significantly increased. Taken together, both functional Tor proteins, Tor1 and Tor2, are essentially required for proper endocytic protein dynamics at the early stage of endocytosis.&lt;/p&gt;","abstract_has_math":false,"creators":["Tenay, Brandon Scott"],"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":2013,"date_issued":"2013-01-01T08:00:00Z","date_published":"2013-01-01T08:00:00Z","updated_at":"2026-07-24T03:16:23Z","subjects":["Tor2","endocytosis","scission","PIP2","Abp1","Biology"],"languages":[],"rights":["© Brandon Scott Tenay"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://bearworks.missouristate.edu/theses/1312","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":["Tenay, Brandon Scott"]}]},{"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":["Tor2","endocytosis","scission","PIP2","Abp1","Biology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© Brandon Scott Tenay"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://bearworks.missouristate.edu/theses/1312"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>Tor2 is an activator of the Rom2/Rho1 pathway that regulates α-factor internalization. Since the recruitment of endocytic proteins such as actin binding proteins and the amphiphysins precedes the internalization of α-factor, I hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. I report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants. Furthermore, I found that the endocytic proteins Rvs167 and Sjl2 are completely mistargeted to the cytoplasm in tor1∆tor2ts double mutant cells. I also demonstrate here that the efficiency of endocytic internalization or scission in all tor mutants was drastically decreased. In agreement with the Sjl2 mislocalization, I found that in tor1∆tor2ts double mutant cells, as well as other tor mutant cells, the overall PIP2 level was dramatically increased. Finally, the cell wall chitin content in tor2ts and tor1∆tor2ts mutant cells was also significantly increased. Taken together, both functional Tor proteins, Tor1 and Tor2, are essentially required for proper endocytic protein dynamics at the early stage of endocytosis.</p>"]},{"key":"dc:title","label":"Title","values":["Inactivation of Tor Proteins Affects the Dynamics of Endocytic Proteins in Early Stage of Endocytosis"]}]}],"canonical_facts":{"dc:contributor":["Kyoungtae Kim"],"dc:creator":["Tenay, Brandon Scott"],"dc:description.abstract":["<p>Tor2 is an activator of the Rom2/Rho1 pathway that regulates α-factor internalization. Since the recruitment of endocytic proteins such as actin binding proteins and the amphiphysins precedes the internalization of α-factor, I hypothesized that loss of Tor function leads to an alteration in the dynamics of the endocytic proteins. I report here that endocytic proteins, Abp1 and Rvs167, are less recruited to endocytic sites not only in tor2 but also tor1 mutants. Furthermore, I found that the endocytic proteins Rvs167 and Sjl2 are completely mistargeted to the cytoplasm in tor1∆tor2ts double mutant cells. I also demonstrate here that the efficiency of endocytic internalization or scission in all tor mutants was drastically decreased. In agreement with the Sjl2 mislocalization, I found that in tor1∆tor2ts double mutant cells, as well as other tor mutant cells, the overall PIP2 level was dramatically increased. Finally, the cell wall chitin content in tor2ts and tor1∆tor2ts mutant cells was also significantly increased. Taken together, both functional Tor proteins, Tor1 and Tor2, are essentially required for proper endocytic protein dynamics at the early stage of endocytosis.</p>"],"dc:identifier":["https://bearworks.missouristate.edu/theses/1312"],"dc:rights":["© Brandon Scott Tenay"],"dc:subject":["Tor2","endocytosis","scission","PIP2","Abp1","Biology"],"dc:title":["Inactivation of Tor Proteins Affects the Dynamics of Endocytic Proteins in Early Stage of Endocytosis"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Masters"],"thesis:degree_name":["Master of Science in Biology"]},"updated_at":"2026-07-24T03:16:23Z"}