{"id":{"repo_id":"debrecen","oai_identifier":"oai:dea.lib.unideb.hu:2437/390853"},"canonical_url":"https://search.dev.ndltd.org/etd/debrecen/oai:dea.lib.unideb.hu:2437/390853","repository":{"repo_id":"debrecen","name":"University of Debrecen","base_url":"https://dea.lib.unideb.hu/server/oai/request"},"display":{"title":"Unraveling the Dynamics of Ser126 Phosphorylation in Paxillin: A Focus on Phosphatase Activity","abstract":"Paxillin is a focal adhesion adaptor protein essential for cell adhesion and migration, regulated by reversible phosphorylation. In endothelial cells, phosphorylation at serine 126 (Ser126) plays a key role in processes like angiogenesis and vascular permeability. This study aimed to identify the phosphatase responsible for dephosphorylating Ser126, a previously unexplored mechanism. Using recombinant paxillin and in vitro kinase assays, we confirmed that PKC phosphorylates Ser126. Inhibition studies in endothelial cells revealed that calcineurin mediates Ser126 dephosphorylation. Phosphorylation at Ser126 enhances paxillin localization to focal adhesions, suggesting a dynamic regulatory mechanism in endothelial cell signaling.","abstract_html":"Paxillin is a focal adhesion adaptor protein essential for cell adhesion and migration, regulated by reversible phosphorylation. In endothelial cells, phosphorylation at serine 126 (Ser126) plays a key role in processes like angiogenesis and vascular permeability. This study aimed to identify the phosphatase responsible for dephosphorylating Ser126, a previously unexplored mechanism. Using recombinant paxillin and in vitro kinase assays, we confirmed that PKC phosphorylates Ser126. Inhibition studies in endothelial cells revealed that calcineurin mediates Ser126 dephosphorylation. Phosphorylation at Ser126 enhances paxillin localization to focal adhesions, suggesting a dynamic regulatory mechanism in endothelial cell signaling.","abstract_has_math":false,"creators":["Pérez Santamaría, Fernanda Estefanía"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":"DE--Általános Orvostudományi Kar","school":null,"contributors":[],"advisors":["Boratkó, Anita"],"committee_chairs":[],"committee_members":[],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-07-27T19:13:55Z","subjects":["Paxillin","Phosphorylation","PKC","Phosphatase","PP2B","Cyclosporine A"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/2437/390853","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Boratkó, Anita"]},{"key":"dc:contributor.department","label":"Department","values":["DE--Általános Orvostudományi Kar"]},{"key":"dc:creator","label":"Author","values":["Pérez Santamaría, Fernanda Estefanía"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2025-06-04T13:01:33Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2025-06-04T13:01:33Z"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Paxillin","Phosphorylation","PKC","Phosphatase","PP2B","Cyclosporine A"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/2437/390853"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Paxillin is a focal adhesion adaptor protein essential for cell adhesion and migration, regulated by reversible phosphorylation. In endothelial cells, phosphorylation at serine 126 (Ser126) plays a key role in processes like angiogenesis and vascular permeability. This study aimed to identify the phosphatase responsible for dephosphorylating Ser126, a previously unexplored mechanism. Using recombinant paxillin and in vitro kinase assays, we confirmed that PKC phosphorylates Ser126. Inhibition studies in endothelial cells revealed that calcineurin mediates Ser126 dephosphorylation. Phosphorylation at Ser126 enhances paxillin localization to focal adhesions, suggesting a dynamic regulatory mechanism in endothelial cell signaling."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["MSc/MA"]},{"key":"dc:title","label":"Title","values":["Unraveling the Dynamics of Ser126 Phosphorylation in Paxillin: A Focus on Phosphatase Activity"]}]}],"canonical_facts":{"dc:contributor.advisor":["Boratkó, Anita"],"dc:contributor.department":["DE--Általános Orvostudományi Kar"],"dc:creator":["Pérez Santamaría, Fernanda Estefanía"],"dc:date.accessioned":["2025-06-04T13:01:33Z"],"dc:date.available":["2025-06-04T13:01:33Z"],"dc:description.abstract":["Paxillin is a focal adhesion adaptor protein essential for cell adhesion and migration, regulated by reversible phosphorylation. In endothelial cells, phosphorylation at serine 126 (Ser126) plays a key role in processes like angiogenesis and vascular permeability. This study aimed to identify the phosphatase responsible for dephosphorylating Ser126, a previously unexplored mechanism. Using recombinant paxillin and in vitro kinase assays, we confirmed that PKC phosphorylates Ser126. Inhibition studies in endothelial cells revealed that calcineurin mediates Ser126 dephosphorylation. Phosphorylation at Ser126 enhances paxillin localization to focal adhesions, suggesting a dynamic regulatory mechanism in endothelial cell signaling."],"dc:description.degree":["MSc/MA"],"dc:identifier.uri":["https://hdl.handle.net/2437/390853"],"dc:language.iso":["en"],"dc:subject":["Paxillin","Phosphorylation","PKC","Phosphatase","PP2B","Cyclosporine A"],"dc:title":["Unraveling the Dynamics of Ser126 Phosphorylation in Paxillin: A Focus on Phosphatase Activity"]},"updated_at":"2026-07-27T19:13:55Z"}