{"id":{"repo_id":"utmb","oai_identifier":"oai:utmb-ir.tdl.org:2152.3/800"},"canonical_url":"https://search.dev.ndltd.org/etd/utmb/oai:utmb-ir.tdl.org:2152.3/800","repository":{"repo_id":"utmb","name":"University of Texas Medical Branch","base_url":"https://utmb-ir.tdl.org/server/oai/request"},"display":{"title":"Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer","abstract":"The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project reported UNC-45A mRNA and protein expression elevated in human cell lines derived from breast carcinoma metastases. UNC-45A knockdowns decreased breast cancer cells proliferation and invasion rates. We also indicated that UNC-45A(a) existed as two isoforms – UNC-45A(a) 929 and 944 – in mammalian cells. UNC-45A(a) 929 isoform had a long 5&apos; untranslated region (UTR) and 944 isoform had a specific 15 amino acid sequence close to its N-terminus. Furthermore, we showed that UNC-45A 929 accumulated higher level in human breast cells. More importantly, the ubiquitin-proteasome system degraded endogenous UNC-45A and the 15 amino acid sequence unique to UNC-45A 944 protein mediated rapid turnover in mammalian cells.","abstract_html":"The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project reported UNC-45A mRNA and protein expression elevated in human cell lines derived from breast carcinoma metastases. UNC-45A knockdowns decreased breast cancer cells proliferation and invasion rates. We also indicated that UNC-45A(a) existed as two isoforms – UNC-45A(a) 929 and 944 – in mammalian cells. UNC-45A(a) 929 isoform had a long 5&amp;apos; untranslated region (UTR) and 944 isoform had a specific 15 amino acid sequence close to its N-terminus. Furthermore, we showed that UNC-45A 929 accumulated higher level in human breast cells. More importantly, the ubiquitin-proteasome system degraded endogenous UNC-45A and the 15 amino acid sequence unique to UNC-45A 944 protein mediated rapid turnover in mammalian cells.","abstract_has_math":false,"creators":["Guo, Wei"],"institution":"The University of Texas Medical Branch at Galveston","degree_name":"Cell Biology (Doctoral)","degree_level":"Doctoral","degree_discipline":"Cell Biology","degree_department":null,"school":null,"contributors":[],"advisors":["Boehning, Darren F"],"committee_chairs":[],"committee_members":["Epstein, Henry F","Barral, José M","May, Gregory S","Tang, Shao-Jun"],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-07-24T05:50:54Z","subjects":["UNC-45","myosin","breast cancer","molecular chaperone regulation","protein degradation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2152.3/800","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Boehning, Darren F"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Epstein, Henry F","Barral, José M","May, Gregory S","Tang, Shao-Jun"]},{"key":"dc:creator","label":"Author","values":["Guo, Wei"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2016-11-01T18:12:55Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2016-11-01T18:12:55Z"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Cell Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Cell Biology (Doctoral)"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["The University of Texas Medical Branch at Galveston"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["UNC-45","myosin","breast cancer","molecular chaperone regulation","protein degradation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/2152.3/800"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project reported UNC-45A mRNA and protein expression elevated in human cell lines derived from breast carcinoma metastases. UNC-45A knockdowns decreased breast cancer cells proliferation and invasion rates. We also indicated that UNC-45A(a) existed as two isoforms – UNC-45A(a) 929 and 944 – in mammalian cells. UNC-45A(a) 929 isoform had a long 5&apos; untranslated region (UTR) and 944 isoform had a specific 15 amino acid sequence close to its N-terminus. Furthermore, we showed that UNC-45A 929 accumulated higher level in human breast cells. More importantly, the ubiquitin-proteasome system degraded endogenous UNC-45A and the 15 amino acid sequence unique to UNC-45A 944 protein mediated rapid turnover in mammalian cells."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer"]}]}],"canonical_facts":{"dc:contributor.advisor":["Boehning, Darren F"],"dc:contributor.committeemember":["Epstein, Henry F","Barral, José M","May, Gregory S","Tang, Shao-Jun"],"dc:creator":["Guo, Wei"],"dc:date.accessioned":["2016-11-01T18:12:55Z"],"dc:date.available":["2016-11-01T18:12:55Z"],"dc:description.abstract":["The UCS (UNC-45; Cro-1; She4p) domain proteins are highly evolutionarily conserved proteins, from fungi to mammals, which interact with several types of myosin, involving proper myosin functions. Caenorhabditis elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project reported UNC-45A mRNA and protein expression elevated in human cell lines derived from breast carcinoma metastases. UNC-45A knockdowns decreased breast cancer cells proliferation and invasion rates. We also indicated that UNC-45A(a) existed as two isoforms – UNC-45A(a) 929 and 944 – in mammalian cells. UNC-45A(a) 929 isoform had a long 5&apos; untranslated region (UTR) and 944 isoform had a specific 15 amino acid sequence close to its N-terminus. Furthermore, we showed that UNC-45A 929 accumulated higher level in human breast cells. More importantly, the ubiquitin-proteasome system degraded endogenous UNC-45A and the 15 amino acid sequence unique to UNC-45A 944 protein mediated rapid turnover in mammalian cells."],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["http://hdl.handle.net/2152.3/800"],"dc:subject":["UNC-45","myosin","breast cancer","molecular chaperone regulation","protein degradation"],"dc:title":["Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer"],"dc:type":["Thesis"],"thesis:degree_discipline":["Cell Biology"],"thesis:degree_level":["Doctoral"],"thesis:degree_name":["Cell Biology (Doctoral)"],"thesis:institution_name":["The University of Texas Medical Branch at Galveston"]},"updated_at":"2026-07-24T05:50:54Z"}