Akirin is a highly conserved protein that has been linked to myogenesis, cardiomyogenisis, and innate immunity. This investigation focused on Akirin in two different aspects, developmentally and subcellularly. Developmentally, we focused on further characterization of Akirin’s role in embryonic musculature development through its genetic interaction with the basal transcription factor, Taf4. We did this by analyzing muscle patterning in akirin, taf4 double heterozygous mutants. Our data confirm a genetic interaction between akirin and taf4. Subcellularly, we investigated the functionality of an Akirin Nuclear Localization Signal (NLS). Through calcium phosphate transfection of S2 cells and fluorescent imaging, we were able to compare wild-type full-length Akirin protein fused to the Venus fluorescent protein to full length Akirin::Venus fusion protein with alanine mutations in the Akirin NLS to determine if a change in nuclear trafficking patterns occurred. Our data show that all constructs were not able to successfully localize within the nucleus. This could mean that there is a possible interference occurring with the nuclear pore complex, or even nuclear overload occurring.
","abstract_html":"<p>Akirin is a highly conserved protein that has been linked to myogenesis, cardiomyogenisis, and innate immunity. This investigation focused on Akirin in two different aspects, developmentally and subcellularly. Developmentally, we focused on further characterization of Akirin’s role in embryonic musculature development through its genetic interaction with the basal transcription factor, Taf4. We did this by analyzing muscle patterning in <em>akirin</em>, <em>taf4</em> double heterozygous mutants. Our data confirm a genetic interaction between <em>akirin</em> and <em>taf4</em>. Subcellularly, we investigated the functionality of an Akirin Nuclear Localization Signal (NLS). Through calcium phosphate transfection of S2 cells and fluorescent imaging, we were able to compare wild-type full-length Akirin protein fused to the Venus fluorescent protein to full length Akirin::Venus fusion protein with alanine mutations in the Akirin NLS to determine if a change in nuclear trafficking patterns occurred. Our data show that all constructs were not able to successfully localize within the nucleus. This could mean that there is a possible interference occurring with the nuclear pore complex, or even nuclear overload occurring. </p>","abstract_has_math":false,"creators":["Gibson, Samantha"],"institution":null,"degree_name":"Master of Science in Integrative Biology (MSIB)","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Jonathan McMurry","Martin Hudson"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2022,"date_issued":"2022-08-08T07:00:00Z","date_published":"2022-08-08T07:00:00Z","updated_at":"2026-07-24T02:43:58Z","subjects":["Biology","Integrative Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.kennesaw.edu/integrbiol_etd/89","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Jonathan McMurry","Martin Hudson"]},{"key":"dc:creator","label":"Author","values":["Gibson, Samantha"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2027-08-16T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Integrative Biology (MSIB)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology","Integrative Biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.kennesaw.edu/integrbiol_etd/89"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Akirin is a highly conserved protein that has been linked to myogenesis, cardiomyogenisis, and innate immunity. This investigation focused on Akirin in two different aspects, developmentally and subcellularly. Developmentally, we focused on further characterization of Akirin’s role in embryonic musculature development through its genetic interaction with the basal transcription factor, Taf4. We did this by analyzing muscle patterning in akirin, taf4 double heterozygous mutants. Our data confirm a genetic interaction between akirin and taf4. Subcellularly, we investigated the functionality of an Akirin Nuclear Localization Signal (NLS). Through calcium phosphate transfection of S2 cells and fluorescent imaging, we were able to compare wild-type full-length Akirin protein fused to the Venus fluorescent protein to full length Akirin::Venus fusion protein with alanine mutations in the Akirin NLS to determine if a change in nuclear trafficking patterns occurred. Our data show that all constructs were not able to successfully localize within the nucleus. This could mean that there is a possible interference occurring with the nuclear pore complex, or even nuclear overload occurring.
"]},{"key":"dc:title","label":"Title","values":["Investigation of Akirin Nuclear Localization and the Molecular Interaction between Akirin and Taf4 in Drosophila"]}]}],"canonical_facts":{"dc:contributor":["Jonathan McMurry","Martin Hudson"],"dc:creator":["Gibson, Samantha"],"dc:date.available":["2027-08-16T07:00:00Z"],"dc:description.abstract":["Akirin is a highly conserved protein that has been linked to myogenesis, cardiomyogenisis, and innate immunity. This investigation focused on Akirin in two different aspects, developmentally and subcellularly. Developmentally, we focused on further characterization of Akirin’s role in embryonic musculature development through its genetic interaction with the basal transcription factor, Taf4. We did this by analyzing muscle patterning in akirin, taf4 double heterozygous mutants. Our data confirm a genetic interaction between akirin and taf4. Subcellularly, we investigated the functionality of an Akirin Nuclear Localization Signal (NLS). Through calcium phosphate transfection of S2 cells and fluorescent imaging, we were able to compare wild-type full-length Akirin protein fused to the Venus fluorescent protein to full length Akirin::Venus fusion protein with alanine mutations in the Akirin NLS to determine if a change in nuclear trafficking patterns occurred. Our data show that all constructs were not able to successfully localize within the nucleus. This could mean that there is a possible interference occurring with the nuclear pore complex, or even nuclear overload occurring.
"],"dc:identifier":["https://digitalcommons.kennesaw.edu/integrbiol_etd/89"],"dc:subject":["Biology","Integrative Biology"],"dc:title":["Investigation of Akirin Nuclear Localization and the Molecular Interaction between Akirin and Taf4 in Drosophila"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science in Integrative Biology (MSIB)"]},"updated_at":"2026-07-24T02:43:58Z"}