{"id":{"repo_id":"siu-theses","oai_identifier":"oai:opensiuc.lib.siu.edu:dissertations-1033"},"canonical_url":"https://search.dev.ndltd.org/etd/siu-theses/oai:opensiuc.lib.siu.edu:dissertations-1033","repository":{"repo_id":"siu-theses","name":"Southern Illinois University","base_url":"https://opensiuc.lib.siu.edu/do/oai/"},"display":{"title":"Identification And Functional Analyses Of Novel Protein Interactions And Post-Translational Modifications For The Transcription Factor Deformed Epidermal Autoregulatory Factor-1.","abstract":"Deformed Epidermal Autoregulatory Factor-1 (DEAF-1) is a transcription factor that binds TTCG motifs and has roles in fetal development, clinical depression and cancer. In order to further our understanding of the DEAF-1 protein, this study characterizes previously unidentified DEAF-1 interacting proteins and post-translational modifications of DEAF-1. A region encompassing the DNA binding domain of DEAF-1 interacts with the C-terminal Bax interacting domain of the Ku70 subunit of the DNA-PK holoenzyme. Ku70 acts as an anti-apoptotic protein through C-terminal domain and so DEAF-1 was assessed for its ability to influence apoptosis after various stimuli. DEAF-1 acted as a pro-apoptotic protein after intrinsic stimuli. Apoptotic activities occurred through a nuclear, DNA independent mechanism and a mutation that eliminated Ku70 interactions also inhibited DEAF-1 pro-apoptotic activities. Analysis of mammalian purified DEAF-1 indicated a number of phosphorylation sites and also a methylated arginine residue. Various assays were performed on mutated forms of DEAF-1 to determine the significance of the modified sites on DEAF-1 functions and properties. Lysine mutation of the methylated arginine site appeared to augment protein-protein interactions with itself and also Ku70. Alanine mutations at three of the identified phosphorylation sites increased DEAF-1 pro-apoptotic activities. In vitro kinase assays identified CDK5 as potential kinase that can phosphorylate DEAF-1. These studies provide new insight into potential functions, properties, and regulation of DEAF-1.","abstract_html":"Deformed Epidermal Autoregulatory Factor-1 (DEAF-1) is a transcription factor that binds TTCG motifs and has roles in fetal development, clinical depression and cancer. In order to further our understanding of the DEAF-1 protein, this study characterizes previously unidentified DEAF-1 interacting proteins and post-translational modifications of DEAF-1. A region encompassing the DNA binding domain of DEAF-1 interacts with the C-terminal Bax interacting domain of the Ku70 subunit of the DNA-PK holoenzyme. Ku70 acts as an anti-apoptotic protein through C-terminal domain and so DEAF-1 was assessed for its ability to influence apoptosis after various stimuli. DEAF-1 acted as a pro-apoptotic protein after intrinsic stimuli. Apoptotic activities occurred through a nuclear, DNA independent mechanism and a mutation that eliminated Ku70 interactions also inhibited DEAF-1 pro-apoptotic activities. Analysis of mammalian purified DEAF-1 indicated a number of phosphorylation sites and also a methylated arginine residue. Various assays were performed on mutated forms of DEAF-1 to determine the significance of the modified sites on DEAF-1 functions and properties. Lysine mutation of the methylated arginine site appeared to augment protein-protein interactions with itself and also Ku70. Alanine mutations at three of the identified phosphorylation sites increased DEAF-1 pro-apoptotic activities. In vitro kinase assays identified CDK5 as potential kinase that can phosphorylate DEAF-1. These studies provide new insight into potential functions, properties, and regulation of DEAF-1.","abstract_has_math":false,"creators":["Jensik, Philip Joseph"],"institution":null,"degree_name":"Doctor of Philosophy","degree_level":"Campus Only Dissertation","degree_discipline":"Molecular, Cellular, and Systemic Physiology","degree_department":null,"school":null,"contributors":["Huggenvik,Jodi"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2009,"date_issued":"2009-01-01T08:00:00Z","date_published":"2009-01-01T08:00:00Z","updated_at":"2026-07-24T04:33:23Z","subjects":["Apoptosis","DEAF-1","Mass Spectrometry","methylation","phosphorylation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://opensiuc.lib.siu.edu/dissertations/33","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Huggenvik,Jodi"]},{"key":"dc:creator","label":"Author","values":["Jensik, Philip Joseph"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2009-11-04T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Molecular, Cellular, and Systemic Physiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Campus Only Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Apoptosis","DEAF-1","Mass Spectrometry","methylation","phosphorylation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://opensiuc.lib.siu.edu/dissertations/33"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Deformed Epidermal Autoregulatory Factor-1 (DEAF-1) is a transcription factor that binds TTCG motifs and has roles in fetal development, clinical depression and cancer. In order to further our understanding of the DEAF-1 protein, this study characterizes previously unidentified DEAF-1 interacting proteins and post-translational modifications of DEAF-1. A region encompassing the DNA binding domain of DEAF-1 interacts with the C-terminal Bax interacting domain of the Ku70 subunit of the DNA-PK holoenzyme. Ku70 acts as an anti-apoptotic protein through C-terminal domain and so DEAF-1 was assessed for its ability to influence apoptosis after various stimuli. DEAF-1 acted as a pro-apoptotic protein after intrinsic stimuli. Apoptotic activities occurred through a nuclear, DNA independent mechanism and a mutation that eliminated Ku70 interactions also inhibited DEAF-1 pro-apoptotic activities. Analysis of mammalian purified DEAF-1 indicated a number of phosphorylation sites and also a methylated arginine residue. Various assays were performed on mutated forms of DEAF-1 to determine the significance of the modified sites on DEAF-1 functions and properties. Lysine mutation of the methylated arginine site appeared to augment protein-protein interactions with itself and also Ku70. Alanine mutations at three of the identified phosphorylation sites increased DEAF-1 pro-apoptotic activities. In vitro kinase assays identified CDK5 as potential kinase that can phosphorylate DEAF-1. These studies provide new insight into potential functions, properties, and regulation of DEAF-1."]},{"key":"dc:title","label":"Title","values":["Identification And Functional Analyses Of Novel Protein Interactions And Post-Translational Modifications For The Transcription Factor Deformed Epidermal Autoregulatory Factor-1."]}]}],"canonical_facts":{"dc:contributor":["Huggenvik,Jodi"],"dc:creator":["Jensik, Philip Joseph"],"dc:date.available":["2009-11-04T08:00:00Z"],"dc:description.abstract":["Deformed Epidermal Autoregulatory Factor-1 (DEAF-1) is a transcription factor that binds TTCG motifs and has roles in fetal development, clinical depression and cancer. In order to further our understanding of the DEAF-1 protein, this study characterizes previously unidentified DEAF-1 interacting proteins and post-translational modifications of DEAF-1. A region encompassing the DNA binding domain of DEAF-1 interacts with the C-terminal Bax interacting domain of the Ku70 subunit of the DNA-PK holoenzyme. Ku70 acts as an anti-apoptotic protein through C-terminal domain and so DEAF-1 was assessed for its ability to influence apoptosis after various stimuli. DEAF-1 acted as a pro-apoptotic protein after intrinsic stimuli. Apoptotic activities occurred through a nuclear, DNA independent mechanism and a mutation that eliminated Ku70 interactions also inhibited DEAF-1 pro-apoptotic activities. Analysis of mammalian purified DEAF-1 indicated a number of phosphorylation sites and also a methylated arginine residue. Various assays were performed on mutated forms of DEAF-1 to determine the significance of the modified sites on DEAF-1 functions and properties. Lysine mutation of the methylated arginine site appeared to augment protein-protein interactions with itself and also Ku70. Alanine mutations at three of the identified phosphorylation sites increased DEAF-1 pro-apoptotic activities. In vitro kinase assays identified CDK5 as potential kinase that can phosphorylate DEAF-1. These studies provide new insight into potential functions, properties, and regulation of DEAF-1."],"dc:identifier":["https://opensiuc.lib.siu.edu/dissertations/33"],"dc:subject":["Apoptosis","DEAF-1","Mass Spectrometry","methylation","phosphorylation"],"dc:title":["Identification And Functional Analyses Of Novel Protein Interactions And Post-Translational Modifications For The Transcription Factor Deformed Epidermal Autoregulatory Factor-1."],"thesis:degree_discipline":["Molecular, Cellular, and Systemic Physiology"],"thesis:degree_level":["Campus Only Dissertation"],"thesis:degree_name":["Doctor of Philosophy"]},"updated_at":"2026-07-24T04:33:23Z"}