{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1362262943764808192.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1073/pnas.0600895103"}},{"identifier":{"@type":"URI","@value":"https://pnas.org/doi/pdf/10.1073/pnas.0600895103"}}],"dc:title":[{"@value":"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: Regulation of aquaporin-2 phosphorylation at two sites"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>\n            Protein phosphorylation plays a key role in vasopressin signaling in the renal-collecting duct. Large-scale identification and quantification of phosphorylation events triggered by vasopressin is desirable to gain a comprehensive systems-level understanding of this process. We carried out phosphoproteomic analysis of rat inner medullary collecting duct cells by using a combination of phosphopeptide enrichment by immobilized metal affinity chromatography and phosphorylation site identification by liquid chromatography-mass spectrometry\n            <jats:sup>n</jats:sup>\n            neutral loss scanning. A total of 714 phosphorylation sites on 223 unique phosphoproteins were identified from inner medullary collecting duct samples treated short-term with either calyculin A or vasopressin. A number of proteins involved in cytoskeletal reorganization, vesicle trafficking, and transcriptional regulation were identified. Previously unidentified phosphorylation sites were found for membrane proteins essential to collecting duct physiology, including eight sites among aquaporin-2 (AQP2), aquaporin-4, and urea transporter isoforms A1 and A3. Through label-free quantification of phosphopeptides, we identified a number of proteins that significantly changed phosphorylation state in response to short-term vasopressin treatment: AQP2, Bclaf1, LRRC47, Rgl3, and SAFB2. In the presence of vasopressin, AQP2 monophosphorylated at S256 and diphosphorylated AQP2 (pS256/261) increased in abundance, whereas AQP2 monophosphorylated at S261 decreased, raising the possibility that both sites are involved in vasopressin-dependent AQP2 trafficking. This study reveals the practicality of liquid chromotography-mass spectrometry\n            <jats:sup>n</jats:sup>\n            neutral loss scanning for large-scale identification and quantification of protein phosphorylation in the analysis of cell signaling in a native mammalian system.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380857673009309056","@type":"Researcher","foaf:name":[{"@value":"Jason D. Hoffert"}],"jpcoar:affiliationName":[{"@value":"National Heart, Lung, and Blood Institute, Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857673009309060","@type":"Researcher","foaf:name":[{"@value":"Trairak Pisitkun"}],"jpcoar:affiliationName":[{"@value":"National Heart, Lung, and Blood Institute, Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857673009309058","@type":"Researcher","foaf:name":[{"@value":"Guanghui Wang"}],"jpcoar:affiliationName":[{"@value":"National Heart, Lung, and Blood Institute, Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857673009309059","@type":"Researcher","foaf:name":[{"@value":"Rong-Fong Shen"}],"jpcoar:affiliationName":[{"@value":"National Heart, Lung, and Blood Institute, Bethesda, MD 20892"}]},{"@id":"https://cir.nii.ac.jp/crid/1380857673009309057","@type":"Researcher","foaf:name":[{"@value":"Mark A. Knepper"}],"jpcoar:affiliationName":[{"@value":"National Heart, Lung, and Blood Institute, Bethesda, MD 20892"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00278424"},{"@type":"EISSN","@value":"10916490"}],"prism:publicationName":[{"@value":"Proceedings of the National Academy of Sciences"}],"dc:publisher":[{"@value":"Proceedings of the National Academy of Sciences"}],"prism:publicationDate":"2006-05-02","prism:volume":"103","prism:number":"18","prism:startingPage":"7159","prism:endingPage":"7164"},"reviewed":"false","url":[{"@id":"https://pnas.org/doi/pdf/10.1073/pnas.0600895103"}],"createdAt":"2006-04-26","modifiedAt":"2022-04-12","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050001335829988224","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Significance of Ser-188 in human mitochondrial NAD kinase as determined by phosphomimetic and phosphoresistant amino-acid substitutions."}]},{"@id":"https://cir.nii.ac.jp/crid/1360004232001736704","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Aquaporin-2 Ser-261 phosphorylation is regulated in combination with Ser-256 and Ser-269 phosphorylation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004232352077696","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Aquaporin 2: From its discovery to molecular structure and medical implications"}]},{"@id":"https://cir.nii.ac.jp/crid/1360016863446009856","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Calcium-dependent protein kinase 16 phosphorylates and activates the aquaporin PIP2;2 to regulate reversible flower opening in\n                    <i>Gentiana scabra</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1360285706909488640","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Regulation of Aquaporins by Vasopressin in the Kidney"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567186282025600","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Characterization of urinary exosomal release of aquaporin-1 and -2 after renal ischemia-reperfusion in rats"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092752440576","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Chlorpromazine Induces Basolateral Aquaporin-2 Accumulation via F-Actin Depolymerization and Blockade of Endocytosis in Renal Epithelial Cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1360584341838064512","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Data resource: vasopressin-regulated protein phosphorylation sites in the collecting duct"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848656932024960","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Ser-261 phospho-regulation is involved in pS256 and pS269-mediated aquaporin-2 apical translocation"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848661910807168","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Two isoforms of aquaporin 2 responsive to hypertonic stress in bottlenose dolphin"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206413362304","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"<b>Phosphorylation and dephosphorylation of aquaporin-2 at serine 269 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