{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86656"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86656","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Identification and Characterization of Pat-6/actopaxin in Caenorhabditis Elegans Body Wall Muscle","abstract":"In addition, I identified PAT-4/ILK and a novel protein, K10B2.5, as putative binding partners of PAT-6/actopaxin. PAT-6/actopaxin and PAT-4/ILK colocalize in vivo, forming a multi-protein complex with UNC-112. The accumulation of PAT-6/actopaxin in body wall muscle cells requires PAT-4/ILK kinase domain. K10B2.5 binds PAT-6/actopaxin in yeast two-hybrid assays, and also colocalizes with PAT-6/actopaxin to muscle attachment sites.","abstract_html":"In addition, I identified PAT-4/ILK and a novel protein, K10B2.5, as putative binding partners of PAT-6/actopaxin. PAT-6/actopaxin and PAT-4/ILK colocalize in vivo, forming a multi-protein complex with UNC-112. The accumulation of PAT-6/actopaxin in body wall muscle cells requires PAT-4/ILK kinase domain. K10B2.5 binds PAT-6/actopaxin in yeast two-hybrid assays, and also colocalizes with PAT-6/actopaxin to muscle attachment sites.","abstract_has_math":false,"creators":["Lin, Xinyi"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Benjamin D. Williams"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-28T15:17:12Z","date_published":"2015-09-28T15:17:12Z","updated_at":"2026-07-22T22:26:27Z","subjects":["Biology, Cell"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3101907"],"render_values":[{"text":"(MiAaPQ)AAI3101907","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/86656","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Benjamin D. 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PAT-6/actopaxin and PAT-4/ILK colocalize in vivo, forming a multi-protein complex with UNC-112. The accumulation of PAT-6/actopaxin in body wall muscle cells requires PAT-4/ILK kinase domain. K10B2.5 binds PAT-6/actopaxin in yeast two-hybrid assays, and also colocalizes with PAT-6/actopaxin to muscle attachment sites.","Made available in DSpace on 2015-09-28T15:17:12Z (GMT). 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PAT-6/actopaxin and PAT-4/ILK colocalize in vivo, forming a multi-protein complex with UNC-112. The accumulation of PAT-6/actopaxin in body wall muscle cells requires PAT-4/ILK kinase domain. K10B2.5 binds PAT-6/actopaxin in yeast two-hybrid assays, and also colocalizes with PAT-6/actopaxin to muscle attachment sites.","Made available in DSpace on 2015-09-28T15:17:12Z (GMT). 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