Selective autophagy, induced by cellular stresses, degrades/recycles a specific cargo. Ithelps prevent diseases like Parkinson’s, Huntington's, cancer, and bacterial infections. It involves the formation of an autophagosome, a double-membrane vesicle that takes the cargo to the vacuole/lysosome for degradation. Atg11, the central organizer of selective autophagy, acts as a scaffold protein, interacting with Atg9, Atg1 and other Atg proteins. Our research focuses on finding mutations in Atg11 that specifically disrupt its interaction with Atg9 without affecting its dimerization or interaction with Atg1. We targeted residues 455-535 of Atg11 as a putative Atg9 interaction site, performing mutagenesis on four key residues in this region. The quadruple mutant (Y468A, D516A, L517A, L526A) disrupted Atg11 and Atg9 interaction. However, Y468A, L526A did not, while D516A, L517A showed only partial disruption. We aim to further investigate other potential residues within this region that may be crucial for Atg11 and Atg9 interaction.
","abstract_html":"<p>Selective autophagy, induced by cellular stresses, degrades/recycles a specific cargo. Ithelps prevent diseases like Parkinson’s, Huntington's, cancer, and bacterial infections. It involves the formation of an autophagosome, a double-membrane vesicle that takes the cargo to the vacuole/lysosome for degradation. Atg11, the central organizer of selective autophagy, acts as a scaffold protein, interacting with Atg9, Atg1 and other Atg proteins. Our research focuses on finding mutations in Atg11 that specifically disrupt its interaction with Atg9 without affecting its dimerization or interaction with Atg1. We targeted residues 455-535 of Atg11 as a putative Atg9 interaction site, performing mutagenesis on four key residues in this region. The quadruple mutant (Y468A, D516A, L517A, L526A) disrupted Atg11 and Atg9 interaction. However, Y468A, L526A did not, while D516A, L517A showed only partial disruption. We aim to further investigate other potential residues within this region that may be crucial for Atg11 and Atg9 interaction.</p>","abstract_has_math":false,"creators":["Sherpa, Chimi Dolker"],"institution":null,"degree_name":"Master of Science (MS)","degree_level":"Open Access Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Steven K Backues, Ph.D.","Brittany Albaugh, Ph.D.","Hedeel Evans, Ph. D."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2024,"date_issued":"2024-01-01T08:00:00Z","date_published":"2024-01-01T08:00:00Z","updated_at":"2026-07-24T02:17:53Z","subjects":["Atg11 and Atg9 interaction","Autophagosome","Autophagy","Co-immunoprecipitation","Yeast-2-Hybrid","Biochemistry","Biochemistry, Biophysics, and Structural Biology","Biology","Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.emich.edu/theses/1266","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Steven K Backues, Ph.D.","Brittany Albaugh, Ph.D.","Hedeel Evans, Ph. D."]},{"key":"dc:creator","label":"Author","values":["Sherpa, Chimi Dolker"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2025-01-31T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Open Access Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science (MS)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Atg11 and Atg9 interaction","Autophagosome","Autophagy","Co-immunoprecipitation","Yeast-2-Hybrid","Biochemistry","Biochemistry, Biophysics, and Structural Biology","Biology","Chemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.emich.edu/theses/1266"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Selective autophagy, induced by cellular stresses, degrades/recycles a specific cargo. Ithelps prevent diseases like Parkinson’s, Huntington's, cancer, and bacterial infections. It involves the formation of an autophagosome, a double-membrane vesicle that takes the cargo to the vacuole/lysosome for degradation. Atg11, the central organizer of selective autophagy, acts as a scaffold protein, interacting with Atg9, Atg1 and other Atg proteins. Our research focuses on finding mutations in Atg11 that specifically disrupt its interaction with Atg9 without affecting its dimerization or interaction with Atg1. We targeted residues 455-535 of Atg11 as a putative Atg9 interaction site, performing mutagenesis on four key residues in this region. The quadruple mutant (Y468A, D516A, L517A, L526A) disrupted Atg11 and Atg9 interaction. However, Y468A, L526A did not, while D516A, L517A showed only partial disruption. We aim to further investigate other potential residues within this region that may be crucial for Atg11 and Atg9 interaction.
"]},{"key":"dc:title","label":"Title","values":["Atg11 and Atg9 interaction in selective autophagy"]}]}],"canonical_facts":{"dc:contributor":["Steven K Backues, Ph.D.","Brittany Albaugh, Ph.D.","Hedeel Evans, Ph. D."],"dc:creator":["Sherpa, Chimi Dolker"],"dc:date.available":["2025-01-31T08:00:00Z"],"dc:description.abstract":["Selective autophagy, induced by cellular stresses, degrades/recycles a specific cargo. Ithelps prevent diseases like Parkinson’s, Huntington's, cancer, and bacterial infections. It involves the formation of an autophagosome, a double-membrane vesicle that takes the cargo to the vacuole/lysosome for degradation. Atg11, the central organizer of selective autophagy, acts as a scaffold protein, interacting with Atg9, Atg1 and other Atg proteins. Our research focuses on finding mutations in Atg11 that specifically disrupt its interaction with Atg9 without affecting its dimerization or interaction with Atg1. We targeted residues 455-535 of Atg11 as a putative Atg9 interaction site, performing mutagenesis on four key residues in this region. The quadruple mutant (Y468A, D516A, L517A, L526A) disrupted Atg11 and Atg9 interaction. However, Y468A, L526A did not, while D516A, L517A showed only partial disruption. We aim to further investigate other potential residues within this region that may be crucial for Atg11 and Atg9 interaction.
"],"dc:identifier":["https://commons.emich.edu/theses/1266"],"dc:subject":["Atg11 and Atg9 interaction","Autophagosome","Autophagy","Co-immunoprecipitation","Yeast-2-Hybrid","Biochemistry","Biochemistry, Biophysics, and Structural Biology","Biology","Chemistry"],"dc:title":["Atg11 and Atg9 interaction in selective autophagy"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Open Access Thesis"],"thesis:degree_name":["Master of Science (MS)"]},"updated_at":"2026-07-24T02:17:53Z"}