{"id":{"repo_id":"purdue-thes","oai_identifier":"oai:docs.lib.purdue.edu:open_access_dissertations-2485"},"canonical_url":"https://search.dev.ndltd.org/etd/purdue-thes/oai:docs.lib.purdue.edu:open_access_dissertations-2485","repository":{"repo_id":"purdue-thes","name":"Purdue University","base_url":"https://docs.lib.purdue.edu/do/oai/"},"display":{"title":"INSIGHTS INTO SUBSTRATE RECOGNITION BY THE ANAPHASE PROMOTING COMPLEX (APC)","abstract":"Mitotic exit depends on the proper degradation of numerous cell cycle-regulated proteins, which is executed by an E3 ubiquitin ligase called the anaphase promoting complex (APC). APC adds polyubiquitin chains to numerous substrates, which leads to their subsequent degradation in late mitosis and G1 phase. The selective and timely recognition and degradation of APC substrates is essential for proper cell cycle progression and maintenance of genome stability. However, a key question is how APC specifically recognizes such a diversity of substrates. The activation of APC requires binding to one of its co-activators, Cdh1 or Cdc20. The co-activators directly facilitate APC enzymatic activity, but also contribute to the highly selective recognition of substrates via binding to degrons, such as the destruction box (D-box), KEN-box, and ABBA motif. However, not all substrates contain these degrons. Moreover, D- and KEN-box sequences are found in many proteins that are clearly not APC substrates, indicating that additional factors must contribute to recognition of these degrons.","abstract_html":"Mitotic exit depends on the proper degradation of numerous cell cycle-regulated proteins, which is executed by an E3 ubiquitin ligase called the anaphase promoting complex (APC). APC adds polyubiquitin chains to numerous substrates, which leads to their subsequent degradation in late mitosis and G1 phase. The selective and timely recognition and degradation of APC substrates is essential for proper cell cycle progression and maintenance of genome stability. However, a key question is how APC specifically recognizes such a diversity of substrates. The activation of APC requires binding to one of its co-activators, Cdh1 or Cdc20. The co-activators directly facilitate APC enzymatic activity, but also contribute to the highly selective recognition of substrates via binding to degrons, such as the destruction box (D-box), KEN-box, and ABBA motif. However, not all substrates contain these degrons. Moreover, D- and KEN-box sequences are found in many proteins that are clearly not APC substrates, indicating that additional factors must contribute to recognition of these degrons.","abstract_has_math":false,"creators":["Qin, Liang"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":["Mark C Hall","Xiaoqi Liu","Sandra Rossie","Clifford Weil"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-01-01T08:00:00Z","date_published":"2016-01-01T08:00:00Z","updated_at":"2026-07-24T03:54:31Z","subjects":["APC","Cdh1","D-box","KEN-box"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://docs.lib.purdue.edu/open_access_dissertations/1269","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Mark C Hall","Xiaoqi Liu","Sandra Rossie","Clifford Weil"]},{"key":"dc:creator","label":"Author","values":["Qin, Liang"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["APC","Cdh1","D-box","KEN-box"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://docs.lib.purdue.edu/open_access_dissertations/1269"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Mitotic exit depends on the proper degradation of numerous cell cycle-regulated proteins, which is executed by an E3 ubiquitin ligase called the anaphase promoting complex (APC). APC adds polyubiquitin chains to numerous substrates, which leads to their subsequent degradation in late mitosis and G1 phase. The selective and timely recognition and degradation of APC substrates is essential for proper cell cycle progression and maintenance of genome stability. However, a key question is how APC specifically recognizes such a diversity of substrates. The activation of APC requires binding to one of its co-activators, Cdh1 or Cdc20. The co-activators directly facilitate APC enzymatic activity, but also contribute to the highly selective recognition of substrates via binding to degrons, such as the destruction box (D-box), KEN-box, and ABBA motif. However, not all substrates contain these degrons. Moreover, D- and KEN-box sequences are found in many proteins that are clearly not APC substrates, indicating that additional factors must contribute to recognition of these degrons."]},{"key":"dc:title","label":"Title","values":["INSIGHTS INTO SUBSTRATE RECOGNITION BY THE ANAPHASE PROMOTING COMPLEX (APC)"]}]}],"canonical_facts":{"dc:contributor":["Mark C Hall","Xiaoqi Liu","Sandra Rossie","Clifford Weil"],"dc:creator":["Qin, Liang"],"dc:description.abstract":["Mitotic exit depends on the proper degradation of numerous cell cycle-regulated proteins, which is executed by an E3 ubiquitin ligase called the anaphase promoting complex (APC). APC adds polyubiquitin chains to numerous substrates, which leads to their subsequent degradation in late mitosis and G1 phase. The selective and timely recognition and degradation of APC substrates is essential for proper cell cycle progression and maintenance of genome stability. However, a key question is how APC specifically recognizes such a diversity of substrates. The activation of APC requires binding to one of its co-activators, Cdh1 or Cdc20. The co-activators directly facilitate APC enzymatic activity, but also contribute to the highly selective recognition of substrates via binding to degrons, such as the destruction box (D-box), KEN-box, and ABBA motif. However, not all substrates contain these degrons. Moreover, D- and KEN-box sequences are found in many proteins that are clearly not APC substrates, indicating that additional factors must contribute to recognition of these degrons."],"dc:identifier":["https://docs.lib.purdue.edu/open_access_dissertations/1269"],"dc:subject":["APC","Cdh1","D-box","KEN-box"],"dc:title":["INSIGHTS INTO SUBSTRATE RECOGNITION BY THE ANAPHASE PROMOTING COMPLEX (APC)"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T03:54:31Z"}