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dc.contributor.authorConner, MT
dc.contributor.authorConner, AC
dc.contributor.authorBland, CE
dc.contributor.authorTaylor, LHJ
dc.contributor.authorBrown, JEP
dc.contributor.authorParri, HR
dc.contributor.authorBill, RM
dc.date.accessioned2020-09-07T11:45:54Z
dc.date.available2020-09-07T11:45:54Z
dc.date.issued2012-02-09
dc.identifier.citationConner, M. T., Conner, Alex C., Bland, C. E., Taylor, Luke H. J., Brown, J. E. P., Parri, H. R. and Bill, R. M. (2012) Rapid aquaporin translocation regulates cellular water flow : Mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channel. Journal of Biological Chemistry, Vol.287 (No.14). pp. 11516-11525. doi:10.1074/jbc.M111.329219en
dc.identifier.issn0021-9258en
dc.identifier.pmid22334691 (pubmed)
dc.identifier.doi10.1074/jbc.M111.329219en
dc.identifier.urihttp://hdl.handle.net/2436/623601
dc.descriptionThis is an accepted manuscript of an article published by American Society for Biochemistry and Molecular Biology in Journal of Biological Chemistry on 09/02/2012, available online; https://www.jbc.org/content/287/14/11516 The accepted version of the publication may differ from the final published version.en
dc.description.abstractThe control of cellular water flow is mediated by the aquaporin (AQP) family of membrane proteins. The structural features of the family and the mechanism of selective water passage through the AQP pore are established, but there remains a gap in our knowledge of how water transport is regulated. Two broad possibilities exist. One is controlling the passage of water through the AQP pore, but this only has been observed as a phenomenon in some plant and microbial AQPs. An alternative is controlling the number of AQPs in the cell membrane. Here, we describe a novel pathway in mammalian cells whereby a hypotonic stimulus directly induces intracellular calcium elevations through transient receptor potential channels, which trigger AQP1 translocation. This translocation, which has a direct role in cell volume regulation, occurs within 30 s and is dependent on calmodulin activation and phosphorylation of AQP1 at two threonine residues by protein kinase C. This direct mechanism provides a rationale for the changes in water transport that are required in response to constantly changing local cellular water availability. Moreover, because calcium is a pluripotent and ubiquitous second messenger in biological systems, the discovery of its role in the regulation of AQP translocation has ramifications for diverse physiological and pathophysiological processes, as well as providing an explanation for the rapid regulation of water flow that is necessary for cell homeostasis. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.en
dc.description.sponsorshipThis work was supported by European Commission Framework Programme 7 Grant 201924 EDICT (to R. M. B.).en
dc.formatapplication/pdfen
dc.languageeng
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttps://www.jbc.org/content/287/14/11516en
dc.rightsLicence for published version: Creative Commons Attribution-NonCommercial 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/
dc.subjectaquaporinen
dc.subjectcalcium channelsen
dc.subjectcellular regulationen
dc.subjectmembrane traffickingen
dc.subjectphosphorylationen
dc.subjectwater channelen
dc.subjecthomeostasisen
dc.subjecthypotonicityen
dc.subject.meshAstrocytes
dc.subject.meshIntracellular Space
dc.subject.meshAnimals
dc.subject.meshHumans
dc.subject.meshRats
dc.subject.meshCalcium
dc.subject.meshWater
dc.subject.meshProtein Kinase C
dc.subject.meshCalmodulin
dc.subject.meshCell Size
dc.subject.meshOsmosis
dc.subject.meshProtein Transport
dc.subject.meshPhosphorylation
dc.subject.meshHomeostasis
dc.subject.meshKinetics
dc.subject.meshTRPC Cation Channels
dc.subject.meshAquaporin 1
dc.subject.meshHEK293 Cells
dc.titleRapid aquaporin translocation regulates cellular water flow: Mechanism of hypotonicity-induced subcellular localization of aquaporin 1 water channelen
dc.typeJournal articleen
dc.identifier.eissn1083-351X
dc.identifier.journalJournal of Biological Chemistryen
dc.date.updated2020-08-28T08:13:29Z
dc.contributor.institutionSchool of Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham B4 7ET, United Kingdom.
pubs.place-of-publicationUnited States
dc.date.accepted2012-01-23
rioxxterms.funderEuropean Commission FP7en
rioxxterms.identifier.projectFP7_en
rioxxterms.versionVoRen
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by-nc/4.0/en
rioxxterms.licenseref.startdate2020-09-07en
dc.source.volume287
dc.source.issue14
dc.source.beginpage11516
dc.source.endpage11525
dc.description.versionPublished version
refterms.dateFCD2020-09-07T11:44:56Z
refterms.versionFCDVoR
refterms.dateFOA2020-09-07T11:45:55Z


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Licence for published version: Creative Commons Attribution-NonCommercial 4.0 International
Except where otherwise noted, this item's license is described as Licence for published version: Creative Commons Attribution-NonCommercial 4.0 International