{"id":{"repo_id":"vcu","oai_identifier":"oai:scholarscompass.vcu.edu:etd-2471"},"canonical_url":"https://search.dev.ndltd.org/etd/vcu/oai:scholarscompass.vcu.edu:etd-2471","repository":{"repo_id":"vcu","name":"Virginia Commonwealth University","base_url":"https://scholarscompass.vcu.edu/do/oai/"},"display":{"title":"Calcium/Calmodulin Dependent Protein Kinase Type-II Associates with Flightless-I to Influence its Nuclear Localization","abstract":"Ca2+/calmodulin-dependent protein kinase type-II (CaMK-II) is a Ser/Thr protein kinase regulated by Ca2+ and Calmodulin. It is a highly conserved and broadly expressed enzyme and has a unique structure and dynamic regulation. It has the ability to remain active in the absence of Ca 2+ as a result of Ca2+ dependent autophosphorylation. CaMK-II phospliorylates proteins involved in neurotransmitter secretion, long term potentiation, cytoskeletal dynamics, gene transcription, and cell motility. To support existing and identify new intracellular roles of CaMK-II, potential binding partners were identified. This was accomplished by transfecting and purifying \"FLAG-tagged\" CaMK-II's (α, βE, δC, and δE). CaMK-II associated proteins were then identified using tandem mass spectrometry. Known binding partners were identified using this approach, including CaMK-II and calmodulin, verifying the approach's validity. Additionally several unexpected but interesting proteins were identified, including the gelsolin related actin binding protein, Flightless-I. Fli-I is an actin binding and capping protein that also functions as a transcriptional coactivator. The CaMK-II-Fli-I interaction was confirmed with endogenous (un-tagged) proteins. The association and localization of Fli-I are dependent on CaMK-II's activity state, although Fli-I is not a substrate of CaMK-II. When CaMK-II is inhibited, Fli-I translocates to the nucleus. Conversely when CaMK-II is artificially activated using a Ca2+ ionophore, Fli-I returns to the cytosol. The discovery of this reversible interaction epresents a potentially new CaMK-II regulated pathway and likely serves as a link between Ca2+ based signal transduction pathways and regulation of the actin component of the cytoskeleton and transcription.","abstract_html":"Ca2+/calmodulin-dependent protein kinase type-II (CaMK-II) is a Ser/Thr protein kinase regulated by Ca2+ and Calmodulin. It is a highly conserved and broadly expressed enzyme and has a unique structure and dynamic regulation. It has the ability to remain active in the absence of Ca 2+ as a result of Ca2+ dependent autophosphorylation. CaMK-II phospliorylates proteins involved in neurotransmitter secretion, long term potentiation, cytoskeletal dynamics, gene transcription, and cell motility. To support existing and identify new intracellular roles of CaMK-II, potential binding partners were identified. This was accomplished by transfecting and purifying "FLAG-tagged" CaMK-II's (α, βE, δC, and δE). CaMK-II associated proteins were then identified using tandem mass spectrometry. Known binding partners were identified using this approach, including CaMK-II and calmodulin, verifying the approach's validity. Additionally several unexpected but interesting proteins were identified, including the gelsolin related actin binding protein, Flightless-I. Fli-I is an actin binding and capping protein that also functions as a transcriptional coactivator. The CaMK-II-Fli-I interaction was confirmed with endogenous (un-tagged) proteins. The association and localization of Fli-I are dependent on CaMK-II's activity state, although Fli-I is not a substrate of CaMK-II. When CaMK-II is inhibited, Fli-I translocates to the nucleus. Conversely when CaMK-II is artificially activated using a Ca2+ ionophore, Fli-I returns to the cytosol. The discovery of this reversible interaction epresents a potentially new CaMK-II regulated pathway and likely serves as a link between Ca2+ based signal transduction pathways and regulation of the actin component of the cytoskeleton and transcription.","abstract_has_math":false,"creators":["Seward, Matthew Edward"],"institution":null,"degree_name":"Master of Science","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Dr. Robert M. Tombes"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2006,"date_issued":"2006-01-01T08:00:00Z","date_published":"2006-01-01T08:00:00Z","updated_at":"2026-07-24T05:55:25Z","subjects":["cytoskeleton","Calmodulin","signal transduction pathways","Flightless-I","CaMK-II","Biology","Life Sciences"],"languages":[],"rights":["© The Author"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarscompass.vcu.edu/etd/1472"],"render_values":[{"text":"https://scholarscompass.vcu.edu/etd/1472","href":"https://scholarscompass.vcu.edu/etd/1472","code":true}]}]},"links":{"outbound_url":"https://doi.org/10.25772/Z8QS-0J91","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dr. Robert M. 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It is a highly conserved and broadly expressed enzyme and has a unique structure and dynamic regulation. It has the ability to remain active in the absence of Ca 2+ as a result of Ca2+ dependent autophosphorylation. CaMK-II phospliorylates proteins involved in neurotransmitter secretion, long term potentiation, cytoskeletal dynamics, gene transcription, and cell motility. To support existing and identify new intracellular roles of CaMK-II, potential binding partners were identified. This was accomplished by transfecting and purifying \"FLAG-tagged\" CaMK-II's (α, βE, δC, and δE). CaMK-II associated proteins were then identified using tandem mass spectrometry. Known binding partners were identified using this approach, including CaMK-II and calmodulin, verifying the approach's validity. Additionally several unexpected but interesting proteins were identified, including the gelsolin related actin binding protein, Flightless-I. Fli-I is an actin binding and capping protein that also functions as a transcriptional coactivator. The CaMK-II-Fli-I interaction was confirmed with endogenous (un-tagged) proteins. The association and localization of Fli-I are dependent on CaMK-II's activity state, although Fli-I is not a substrate of CaMK-II. When CaMK-II is inhibited, Fli-I translocates to the nucleus. Conversely when CaMK-II is artificially activated using a Ca2+ ionophore, Fli-I returns to the cytosol. The discovery of this reversible interaction epresents a potentially new CaMK-II regulated pathway and likely serves as a link between Ca2+ based signal transduction pathways and regulation of the actin component of the cytoskeleton and transcription."]},{"key":"dc:title","label":"Title","values":["Calcium/Calmodulin Dependent Protein Kinase Type-II Associates with Flightless-I to Influence its Nuclear Localization"]}]}],"canonical_facts":{"dc:contributor":["Dr. Robert M. Tombes"],"dc:creator":["Seward, Matthew Edward"],"dc:date.available":["2014-07-09T07:00:00Z"],"dc:description.abstract":["Ca2+/calmodulin-dependent protein kinase type-II (CaMK-II) is a Ser/Thr protein kinase regulated by Ca2+ and Calmodulin. It is a highly conserved and broadly expressed enzyme and has a unique structure and dynamic regulation. It has the ability to remain active in the absence of Ca 2+ as a result of Ca2+ dependent autophosphorylation. CaMK-II phospliorylates proteins involved in neurotransmitter secretion, long term potentiation, cytoskeletal dynamics, gene transcription, and cell motility. To support existing and identify new intracellular roles of CaMK-II, potential binding partners were identified. This was accomplished by transfecting and purifying \"FLAG-tagged\" CaMK-II's (α, βE, δC, and δE). CaMK-II associated proteins were then identified using tandem mass spectrometry. Known binding partners were identified using this approach, including CaMK-II and calmodulin, verifying the approach's validity. Additionally several unexpected but interesting proteins were identified, including the gelsolin related actin binding protein, Flightless-I. Fli-I is an actin binding and capping protein that also functions as a transcriptional coactivator. The CaMK-II-Fli-I interaction was confirmed with endogenous (un-tagged) proteins. The association and localization of Fli-I are dependent on CaMK-II's activity state, although Fli-I is not a substrate of CaMK-II. When CaMK-II is inhibited, Fli-I translocates to the nucleus. Conversely when CaMK-II is artificially activated using a Ca2+ ionophore, Fli-I returns to the cytosol. The discovery of this reversible interaction epresents a potentially new CaMK-II regulated pathway and likely serves as a link between Ca2+ based signal transduction pathways and regulation of the actin component of the cytoskeleton and transcription."],"dc:identifier":["https://doi.org/10.25772/Z8QS-0J91","https://scholarscompass.vcu.edu/etd/1472"],"dc:rights":["© The Author"],"dc:subject":["cytoskeleton","Calmodulin","signal transduction pathways","Flightless-I","CaMK-II","Biology","Life Sciences"],"dc:title":["Calcium/Calmodulin Dependent Protein Kinase Type-II Associates with Flightless-I to Influence its Nuclear Localization"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T05:55:25Z"}