{"@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/1361137044022344192.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1074/jbc.272.23.14800"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925819624622?httpAccept=text/xml"}},{"identifier":{"@type":"URI","@value":"https://api.elsevier.com/content/article/PII:S0021925819624622?httpAccept=text/plain"}},{"identifier":{"@type":"URI","@value":"https://syndication.highwire.org/content/doi/10.1074/jbc.272.23.14800"}},{"identifier":{"@type":"PMID","@value":"9169447"}},{"identifier":{"@type":"NAID","@value":"80009750927"}}],"dc:title":[{"@value":"Phosphorylation of Serine 256 Is Required for cAMP-dependent Regulatory Exocytosis of the Aquaporin-2 Water Channel"}],"description":[{"notation":[{"@value":"The aquaporin-2 (AQP2) vasopressin water channel is translocated to the apical membrane upon vasopressin stimulation. Phosphorylation of serine 256 of AQP2 by cAMP-dependent protein kinase has been shown, but its relation to vasopressin-regulated translocation has not been elucidated. To address this question, wild type (WT) AQP2 and a mutant with alanine in place of serine 256 of AQP2 (S256A) were expressed in LLC-PK1 cells by electroporation. Measurements by a stopped-flow light-scattering method revealed that the osmotic water permeability (Pf) of LLC-PK1 cells transfected with WT was 69.6 +/- 6.5 microm/s (24.8 +/- 2.2 microm/s for mock-transfected), and stimulation by 500 microM 8-(4-chlorophenylthio)-cAMP increased the Pf by 85 +/- 12%. When S256A AQP2 was transfected, the cAMP-dependent increase in the Pf was only 8 +/- 5%. After cAMP stimulation, the increase in surface expression of AQP2 determined by surface biotin labeling was 4 +/- 10%, significantly less than that for WT (88 +/- 5%). In addition, an in vivo [32P]orthophosphate labeling assay demonstrated significant phosphorylation of WT AQP2 and only minimal phosphorylation of S256A AQP2 in LLC-PK1 cells. Our results indicated that serine 256 of AQP2 is necessary for regulatory exocytosis and that cAMP-responsive redistribution of AQP2 may be regulated by phosphorylation of AQP2."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1381137044022344193","@type":"Researcher","foaf:name":[{"@value":"Kiyohide Fushimi"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044022344194","@type":"Researcher","foaf:name":[{"@value":"Sei Sasaki"}]},{"@id":"https://cir.nii.ac.jp/crid/1381137044022344192","@type":"Researcher","foaf:name":[{"@value":"Fumiaki Marumo"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00219258"}],"prism:publicationName":[{"@value":"Journal of Biological Chemistry"}],"dc:publisher":[{"@value":"Elsevier BV"}],"prism:publicationDate":"1997-06","prism:volume":"272","prism:number":"23","prism:startingPage":"14800","prism:endingPage":"14804"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["https://www.elsevier.com/tdm/userlicense/1.0/","http://creativecommons.org/licenses/by/4.0/"],"url":[{"@id":"https://api.elsevier.com/content/article/PII:S0021925819624622?httpAccept=text/xml"},{"@id":"https://api.elsevier.com/content/article/PII:S0021925819624622?httpAccept=text/plain"},{"@id":"https://syndication.highwire.org/content/doi/10.1074/jbc.272.23.14800"}],"createdAt":"2002-07-26","modifiedAt":"2021-10-27","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Alanine","dc:title":"Alanine"},{"@id":"https://cir.nii.ac.jp/all?q=Aquaporin%202","dc:title":"Aquaporin 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Site-Directed"},{"@id":"https://cir.nii.ac.jp/all?q=Serine","dc:title":"Serine"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Point%20Mutation","dc:title":"Point Mutation"},{"@id":"https://cir.nii.ac.jp/all?q=Scattering,%20Radiation","dc:title":"Scattering, Radiation"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphorylation","dc:title":"Phosphorylation"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360002218651218176","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling in salivary gland cells"}]},{"@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 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