{"id":{"repo_id":"nus","oai_identifier":"oai:scholarbank.nus.edu.sg:10635/17599"},"canonical_url":"https://search.dev.ndltd.org/etd/nus/oai:scholarbank.nus.edu.sg:10635/17599","repository":{"repo_id":"nus","name":"National University of Singapore","base_url":"https://scholarbank.nus.edu.sg/oai/request"},"display":{"title":"Molecular function and regulation of the Bax-associating protein MOAP-1","abstract":"Bax is a central regulator for controlling the release of apoptogenic factors from mitochondria. MOAP-1 has previously been identified as a Bax-associating protein, but its regulation and functional relationship with Bax in apoptosis signalling remains unclear. In this thesis, MOAP-1 is found to be a short-lived mitochondrial protein due to constitutive degradation by the ubiquitin-proteasome system. MOAP-1 is rapidly up-regulated by multiple apoptotic stimuli through inhibition of its poly-ubiquitination process. Elevation of MOAP-1 levels sensitizes cells to apoptotic stimuli, whereas, cells with stable expression of MOAP-1 siRNAs are resistant to multiple apoptotic stimuli. Remarkably, the effect of recombinant Bax and tBid proteins in stimulating release of cytochrome c from isolated mitochondria is significantly compromised by the depletion of MOAP-1. Identification of MOAP-1 as a mitochondrial effector of Bax and a substrate of the ubiquitin-proteasome pathway would have an important implication for conceptualizing novel therapeutic strategies in combating human diseases.","abstract_html":"Bax is a central regulator for controlling the release of apoptogenic factors from mitochondria. MOAP-1 has previously been identified as a Bax-associating protein, but its regulation and functional relationship with Bax in apoptosis signalling remains unclear. In this thesis, MOAP-1 is found to be a short-lived mitochondrial protein due to constitutive degradation by the ubiquitin-proteasome system. MOAP-1 is rapidly up-regulated by multiple apoptotic stimuli through inhibition of its poly-ubiquitination process. Elevation of MOAP-1 levels sensitizes cells to apoptotic stimuli, whereas, cells with stable expression of MOAP-1 siRNAs are resistant to multiple apoptotic stimuli. Remarkably, the effect of recombinant Bax and tBid proteins in stimulating release of cytochrome c from isolated mitochondria is significantly compromised by the depletion of MOAP-1. Identification of MOAP-1 as a mitochondrial effector of Bax and a substrate of the ubiquitin-proteasome pathway would have an important implication for conceptualizing novel therapeutic strategies in combating human diseases.","abstract_has_math":false,"creators":["FU NAIYANG"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2007,"date_issued":"2007-09-12","date_published":"2007-09-12","updated_at":"2026-07-24T03:31:13Z","subjects":["Apoptosis, mitochondria, Bcl-2 family, MOAP-1, ubiquitin, proteasome"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["FU NAIYANG"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.issued","label":"Date","values":["2007-09-12"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://scholarbank.nus.edu.sg/handle/10635/17599"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Apoptosis, mitochondria, Bcl-2 family, MOAP-1, ubiquitin, proteasome"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://scholarbank.nus.edu.sg/bitstreams/c0fe6f53-55e5-45be-92a8-33c82a2c142c/download"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Bax is a central regulator for controlling the release of apoptogenic factors from mitochondria. MOAP-1 has previously been identified as a Bax-associating protein, but its regulation and functional relationship with Bax in apoptosis signalling remains unclear. In this thesis, MOAP-1 is found to be a short-lived mitochondrial protein due to constitutive degradation by the ubiquitin-proteasome system. MOAP-1 is rapidly up-regulated by multiple apoptotic stimuli through inhibition of its poly-ubiquitination process. Elevation of MOAP-1 levels sensitizes cells to apoptotic stimuli, whereas, cells with stable expression of MOAP-1 siRNAs are resistant to multiple apoptotic stimuli. Remarkably, the effect of recombinant Bax and tBid proteins in stimulating release of cytochrome c from isolated mitochondria is significantly compromised by the depletion of MOAP-1. Identification of MOAP-1 as a mitochondrial effector of Bax and a substrate of the ubiquitin-proteasome pathway would have an important implication for conceptualizing novel therapeutic strategies in combating human diseases."]},{"key":"dc:format.checksum.md5","label":"Dc Format Checksum Md5","values":["552a65271611a6ca6bb8677306d21fe5","f0f0f37c6c401375dd82ae00625d089e"]},{"key":"dc:title","label":"Title","values":["Molecular function and regulation of the Bax-associating protein MOAP-1"]}]}],"canonical_facts":{"dc:creator":["FU NAIYANG"],"dc:date.issued":["2007-09-12"],"dc:description.abstract":["Bax is a central regulator for controlling the release of apoptogenic factors from mitochondria. MOAP-1 has previously been identified as a Bax-associating protein, but its regulation and functional relationship with Bax in apoptosis signalling remains unclear. In this thesis, MOAP-1 is found to be a short-lived mitochondrial protein due to constitutive degradation by the ubiquitin-proteasome system. MOAP-1 is rapidly up-regulated by multiple apoptotic stimuli through inhibition of its poly-ubiquitination process. Elevation of MOAP-1 levels sensitizes cells to apoptotic stimuli, whereas, cells with stable expression of MOAP-1 siRNAs are resistant to multiple apoptotic stimuli. Remarkably, the effect of recombinant Bax and tBid proteins in stimulating release of cytochrome c from isolated mitochondria is significantly compromised by the depletion of MOAP-1. Identification of MOAP-1 as a mitochondrial effector of Bax and a substrate of the ubiquitin-proteasome pathway would have an important implication for conceptualizing novel therapeutic strategies in combating human diseases."],"dc:format.checksum.md5":["552a65271611a6ca6bb8677306d21fe5","f0f0f37c6c401375dd82ae00625d089e"],"dc:identifier.uri":["https://scholarbank.nus.edu.sg/bitstreams/c0fe6f53-55e5-45be-92a8-33c82a2c142c/download"],"dc:relation.isreferencedby":["https://scholarbank.nus.edu.sg/handle/10635/17599"],"dc:subject":["Apoptosis, mitochondria, Bcl-2 family, MOAP-1, ubiquitin, proteasome"],"dc:title":["Molecular function and regulation of the Bax-associating protein MOAP-1"],"dc:type":["Thesis"]},"updated_at":"2026-07-24T03:31:13Z"}