{"id":{"repo_id":"york","oai_identifier":"oai:yorkspace.library.yorku.ca:10315/40981"},"canonical_url":"https://search.dev.ndltd.org/etd/york/oai:yorkspace.library.yorku.ca:10315/40981","repository":{"repo_id":"york","name":"York University","base_url":"https://yorkspace.library.yorku.ca/oai/request"},"display":{"title":"The TAZ Protein Interactome in Striated Muscle","abstract":"Hippo signalling is a prominent regulator of cell proliferation, differentiation, and death. Previously, we characterized the Hippo transcriptional effector TAZ as a repressor of the myogenic differentiation program. Without DNA-binding ability, TAZ function exclusively depends on its protein:protein interaction network. This prompted us to undertake a proteomic-based study aimed at identifying the TAZ interactome in striated muscle cells. Using a novel GFP-Nanotrap based affinity purification approach coupled with LC-MS/MS protein identification, we document a comprehensive list of known and novel TAZ interactome components in myogenic cells. TAZ interacting proteins include components of Hippo signalling: TEAD1-4, LATS1, 14-3-3 proteins. Epigenetic regulators were also represented: NuRD complex, FACT complex, and SWI/SNF complex. We focused on characterizing the TAZ interaction with the Wnt co-repressor TLE3 in myogenic cells. In myogenic cells, TAZ and TLE3 interact and co-localize within the nucleus. Functionally, TAZ and TLE3 repress β-catenin activation, as indicated by the Wnt-responsive TOP FLASH reporter gene system. Depletion of TAZ reduced the degree of TLE3-mediated repression of β-catenin activation. TAZ and TLE3 repressed MyoD-driven activation of the myogenin promoter. Overall, these data demonstrate a role for a TAZ/TLE3 complex in repressing the myogenic differentiation machinery having implications for muscle development and regeneration.","abstract_html":"Hippo signalling is a prominent regulator of cell proliferation, differentiation, and death. Previously, we characterized the Hippo transcriptional effector TAZ as a repressor of the myogenic differentiation program. Without DNA-binding ability, TAZ function exclusively depends on its protein:protein interaction network. This prompted us to undertake a proteomic-based study aimed at identifying the TAZ interactome in striated muscle cells. Using a novel GFP-Nanotrap based affinity purification approach coupled with LC-MS/MS protein identification, we document a comprehensive list of known and novel TAZ interactome components in myogenic cells. TAZ interacting proteins include components of Hippo signalling: TEAD1-4, LATS1, 14-3-3 proteins. Epigenetic regulators were also represented: NuRD complex, FACT complex, and SWI/SNF complex. We focused on characterizing the TAZ interaction with the Wnt co-repressor TLE3 in myogenic cells. In myogenic cells, TAZ and TLE3 interact and co-localize within the nucleus. Functionally, TAZ and TLE3 repress β-catenin activation, as indicated by the Wnt-responsive TOP FLASH reporter gene system. Depletion of TAZ reduced the degree of TLE3-mediated repression of β-catenin activation. TAZ and TLE3 repressed MyoD-driven activation of the myogenin promoter. Overall, these data demonstrate a role for a TAZ/TLE3 complex in repressing the myogenic differentiation machinery having implications for muscle development and regeneration.","abstract_has_math":false,"creators":["Kelebeev, Jonathan"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["McDermott, John Charles"],"committee_chairs":[],"committee_members":[],"year":2023,"date_issued":"2023-03-28","date_published":"2023-03-28","updated_at":"2026-07-24T06:33:43Z","subjects":["Molecular biology","Biochemistry","Cellular biology"],"languages":["en"],"rights":["Author owns copyright, except where explicitly noted. Please contact the author directly with licensing requests."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10315/40981","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["McDermott, John Charles"]},{"key":"dc:creator","label":"Author","values":["Kelebeev, Jonathan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2023-03-28T21:15:56Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2023-03-28T21:15:56Z"]},{"key":"dc:date.issued","label":"Date","values":["2023-03-28"]},{"key":"dc:type","label":"Dc Type","values":["Electronic Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Molecular biology","Biochemistry","Cellular biology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Author owns copyright, except where explicitly noted. Please contact the author directly with licensing requests."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10315/40981"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Hippo signalling is a prominent regulator of cell proliferation, differentiation, and death. Previously, we characterized the Hippo transcriptional effector TAZ as a repressor of the myogenic differentiation program. Without DNA-binding ability, TAZ function exclusively depends on its protein:protein interaction network. This prompted us to undertake a proteomic-based study aimed at identifying the TAZ interactome in striated muscle cells. Using a novel GFP-Nanotrap based affinity purification approach coupled with LC-MS/MS protein identification, we document a comprehensive list of known and novel TAZ interactome components in myogenic cells. TAZ interacting proteins include components of Hippo signalling: TEAD1-4, LATS1, 14-3-3 proteins. Epigenetic regulators were also represented: NuRD complex, FACT complex, and SWI/SNF complex. We focused on characterizing the TAZ interaction with the Wnt co-repressor TLE3 in myogenic cells. In myogenic cells, TAZ and TLE3 interact and co-localize within the nucleus. Functionally, TAZ and TLE3 repress β-catenin activation, as indicated by the Wnt-responsive TOP FLASH reporter gene system. Depletion of TAZ reduced the degree of TLE3-mediated repression of β-catenin activation. TAZ and TLE3 repressed MyoD-driven activation of the myogenin promoter. Overall, these data demonstrate a role for a TAZ/TLE3 complex in repressing the myogenic differentiation machinery having implications for muscle development and regeneration."]},{"key":"dc:title","label":"Title","values":["The TAZ Protein Interactome in Striated Muscle"]}]}],"canonical_facts":{"dc:contributor.advisor":["McDermott, John Charles"],"dc:creator":["Kelebeev, Jonathan"],"dc:date.accessioned":["2023-03-28T21:15:56Z"],"dc:date.available":["2023-03-28T21:15:56Z"],"dc:date.issued":["2023-03-28"],"dc:description.abstract":["Hippo signalling is a prominent regulator of cell proliferation, differentiation, and death. Previously, we characterized the Hippo transcriptional effector TAZ as a repressor of the myogenic differentiation program. Without DNA-binding ability, TAZ function exclusively depends on its protein:protein interaction network. This prompted us to undertake a proteomic-based study aimed at identifying the TAZ interactome in striated muscle cells. Using a novel GFP-Nanotrap based affinity purification approach coupled with LC-MS/MS protein identification, we document a comprehensive list of known and novel TAZ interactome components in myogenic cells. TAZ interacting proteins include components of Hippo signalling: TEAD1-4, LATS1, 14-3-3 proteins. Epigenetic regulators were also represented: NuRD complex, FACT complex, and SWI/SNF complex. We focused on characterizing the TAZ interaction with the Wnt co-repressor TLE3 in myogenic cells. In myogenic cells, TAZ and TLE3 interact and co-localize within the nucleus. Functionally, TAZ and TLE3 repress β-catenin activation, as indicated by the Wnt-responsive TOP FLASH reporter gene system. Depletion of TAZ reduced the degree of TLE3-mediated repression of β-catenin activation. TAZ and TLE3 repressed MyoD-driven activation of the myogenin promoter. Overall, these data demonstrate a role for a TAZ/TLE3 complex in repressing the myogenic differentiation machinery having implications for muscle development and regeneration."],"dc:identifier.uri":["http://hdl.handle.net/10315/40981"],"dc:language":["en"],"dc:rights":["Author owns copyright, except where explicitly noted. Please contact the author directly with licensing requests."],"dc:subject":["Molecular biology","Biochemistry","Cellular biology"],"dc:title":["The TAZ Protein Interactome in Striated Muscle"],"dc:type":["Electronic Thesis or Dissertation"]},"updated_at":"2026-07-24T06:33:43Z"}