{"id":{"repo_id":"wvu","oai_identifier":"oai:researchrepository.wvu.edu:etd-2520"},"canonical_url":"https://search.dev.ndltd.org/etd/wvu/oai:researchrepository.wvu.edu:etd-2520","repository":{"repo_id":"wvu","name":"West Virginia University","base_url":"https://researchrepository.wvu.edu/do/oai/"},"display":{"title":"Determining the effects of phosphorylation on AFAP-110 function","abstract":"As there are over twenty potential PKC phosphorylation sites in AFAP-110 structure, deletional mutagenesis was employed to determine which regions of AFAP-110 are most likely to contain crucial sites for PKC phosphorylation. Our data indicate that functional PKC phosphorylation sites must be localized to the amino acid stretch 266--294 within STK region of AFAP-110. There are four PKC candidate phosphorylation sites in this region; they are being substituted by alanine residues in order to determine their significance in serine/threonine phosphorylation regulation of AFAP-110 function.;Analysis of AFAP-110 amino acid sequence has also revealed that AFAP-110 contains twelve potential 14-3-3 binding sequences. 14-3-3 proteins are a family of small acidic adaptor proteins of dimeric nature that act as molecular scaffolds and/or allosteric regulators in a number of cellular pathways. We have been interested to determine whether 14-3-3 is a binding partner for AFAP-110 in vivo. We determined that AFAP-110 associates with 14-3-3 in vivo, although it still remains unknown whether this association is direct or facilitated by any of a multitude of 14-3-3 binding partners. (Abstract shortened by UMI.).","abstract_html":"As there are over twenty potential PKC phosphorylation sites in AFAP-110 structure, deletional mutagenesis was employed to determine which regions of AFAP-110 are most likely to contain crucial sites for PKC phosphorylation. Our data indicate that functional PKC phosphorylation sites must be localized to the amino acid stretch 266--294 within STK region of AFAP-110. There are four PKC candidate phosphorylation sites in this region; they are being substituted by alanine residues in order to determine their significance in serine/threonine phosphorylation regulation of AFAP-110 function.;Analysis of AFAP-110 amino acid sequence has also revealed that AFAP-110 contains twelve potential 14-3-3 binding sequences. 14-3-3 proteins are a family of small acidic adaptor proteins of dimeric nature that act as molecular scaffolds and/or allosteric regulators in a number of cellular pathways. We have been interested to determine whether 14-3-3 is a binding partner for AFAP-110 in vivo. We determined that AFAP-110 associates with 14-3-3 in vivo, although it still remains unknown whether this association is direct or facilitated by any of a multitude of 14-3-3 binding partners. (Abstract shortened by UMI.).","abstract_has_math":false,"creators":["Cherezova, Lidia Nikolayevna"],"institution":null,"degree_name":"MS","degree_level":"Thesis","degree_discipline":"Microbiology, Immunology, and Cell Biology","degree_department":null,"school":null,"contributors":["Daniel Flynn."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2002,"date_issued":"2002-08-01T07:00:00Z","date_published":"2002-08-01T07:00:00Z","updated_at":"2026-07-24T06:15:47Z","subjects":["Cellular biology","Molecular biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://researchrepository.wvu.edu/etd/1517"],"render_values":[{"text":"https://researchrepository.wvu.edu/etd/1517","href":"https://researchrepository.wvu.edu/etd/1517","code":true}]}]},"links":{"outbound_url":"https://doi.org/10.33915/etd.1517","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Daniel Flynn."]},{"key":"dc:creator","label":"Author","values":["Cherezova, Lidia Nikolayevna"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2019-01-17T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology, Immunology, and Cell Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["MS"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Cellular biology","Molecular biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://doi.org/10.33915/etd.1517","https://researchrepository.wvu.edu/etd/1517"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["As there are over twenty potential PKC phosphorylation sites in AFAP-110 structure, deletional mutagenesis was employed to determine which regions of AFAP-110 are most likely to contain crucial sites for PKC phosphorylation. Our data indicate that functional PKC phosphorylation sites must be localized to the amino acid stretch 266--294 within STK region of AFAP-110. There are four PKC candidate phosphorylation sites in this region; they are being substituted by alanine residues in order to determine their significance in serine/threonine phosphorylation regulation of AFAP-110 function.;Analysis of AFAP-110 amino acid sequence has also revealed that AFAP-110 contains twelve potential 14-3-3 binding sequences. 14-3-3 proteins are a family of small acidic adaptor proteins of dimeric nature that act as molecular scaffolds and/or allosteric regulators in a number of cellular pathways. We have been interested to determine whether 14-3-3 is a binding partner for AFAP-110 in vivo. We determined that AFAP-110 associates with 14-3-3 in vivo, although it still remains unknown whether this association is direct or facilitated by any of a multitude of 14-3-3 binding partners. (Abstract shortened by UMI.)."]},{"key":"dc:title","label":"Title","values":["Determining the effects of phosphorylation on AFAP-110 function"]}]}],"canonical_facts":{"dc:contributor":["Daniel Flynn."],"dc:creator":["Cherezova, Lidia Nikolayevna"],"dc:date.available":["2019-01-17T08:00:00Z"],"dc:description.abstract":["As there are over twenty potential PKC phosphorylation sites in AFAP-110 structure, deletional mutagenesis was employed to determine which regions of AFAP-110 are most likely to contain crucial sites for PKC phosphorylation. Our data indicate that functional PKC phosphorylation sites must be localized to the amino acid stretch 266--294 within STK region of AFAP-110. There are four PKC candidate phosphorylation sites in this region; they are being substituted by alanine residues in order to determine their significance in serine/threonine phosphorylation regulation of AFAP-110 function.;Analysis of AFAP-110 amino acid sequence has also revealed that AFAP-110 contains twelve potential 14-3-3 binding sequences. 14-3-3 proteins are a family of small acidic adaptor proteins of dimeric nature that act as molecular scaffolds and/or allosteric regulators in a number of cellular pathways. We have been interested to determine whether 14-3-3 is a binding partner for AFAP-110 in vivo. We determined that AFAP-110 associates with 14-3-3 in vivo, although it still remains unknown whether this association is direct or facilitated by any of a multitude of 14-3-3 binding partners. (Abstract shortened by UMI.)."],"dc:identifier":["https://doi.org/10.33915/etd.1517","https://researchrepository.wvu.edu/etd/1517"],"dc:subject":["Cellular biology","Molecular biology"],"dc:title":["Determining the effects of phosphorylation on AFAP-110 function"],"thesis:degree_discipline":["Microbiology, Immunology, and Cell Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["MS"]},"updated_at":"2026-07-24T06:15:47Z"}