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dc.contributor.authorKitchen, P
dc.contributor.authorConner, MT
dc.contributor.authorBill, RM
dc.contributor.authorConner, AC
dc.date.accessioned2019-05-13T10:04:43Z
dc.date.available2019-05-13T10:04:43Z
dc.date.issued2016-01-19
dc.identifier.citationKitchen, P., Conner, M. T., Bill, R. M. and Conner, A. C. (2016) Structural determinants of oligomerization of the aquaporin-4 channel, Journal of Biological Chemistry, 29(13), pp. 6858-6871.en
dc.identifier.issn0021-9258en
dc.identifier.pmid26786101
dc.identifier.doi10.1074/jbc.M115.694729en
dc.identifier.urihttp://hdl.handle.net/2436/622343
dc.description.abstract©2016 by The American Society for Biochemistry and Molecular Biology, Inc. The aquaporin (AQP) family of integral membrane protein channels mediate cellular water and solute flow. Although qualitative and quantitative differences in channel permeability, selectivity, subcellular localization, and trafficking responses have been observed for different members of the AQP family, the signature homotetrameric quaternary structure is conserved. Using a variety of biophysical techniques, we show that mutations to an intracellular loop (loop D) of human AQP4 reduce oligomerization. Non-tetrameric AQP4 mutants are unable to relocalize to the plasma membrane in response to changes in extracellular tonicity, despite equivalent constitutive surface expression levels and water permeability to wild-type AQP4. A network of AQP4 loop D hydrogen bonding interactions, identified using molecular dynamics simulations and based on a comparative mutagenic analysis of AQPs 1, 3, and 4, suggest that loop D interactions may provide a general structural framework for tetrameric assembly within theAQPfamily.en
dc.description.sponsorshipSupported by Biotechnology and Biological Sciences Research Council Grants BB/I019960/1, BB/K013319/1, and BB/L502194/1 and Innovative Medicines Joint Undertaking under Grant Agreement 115583 to the ND4BB ENABLE Consortium.en
dc.formatapplication/PDFen
dc.languageeng
dc.language.isoenen
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)en
dc.relation.urlhttp://www.jbc.org/content/291/13/6858en
dc.rightsLicence for published version: Creative Commons Attribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAnimalsen
dc.subjectDogsen
dc.subjectHumansen
dc.subjectEscherichia colien
dc.subjectWateren
dc.subjectRecombinant Proteinsen
dc.subjectCrystallography, X-Rayen
dc.subjectCloning, Molecularen
dc.subjectSequence Alignmenten
dc.subjectGene Expressionen
dc.subjectAmino Acid Sequenceen
dc.subjectProtein Structure, Secondaryen
dc.subjectStructural Homology, Proteinen
dc.subjectProtein Transporten
dc.subjectMutationen
dc.subjectHydrogen Bondingen
dc.subjectOsmolar Concentrationen
dc.subjectMolecular Sequence Dataen
dc.subjectAquaporin 1en
dc.subjectAquaporin 3en
dc.subjectAquaporin 4en
dc.subjectProtein Interaction Domains and Motifsen
dc.subjectProtein Multimerizationen
dc.subjectMolecular Dynamics Simulationen
dc.subjectHEK293 Cellsen
dc.subjectMadin Darby Canine Kidney Cellsen
dc.titleStructural determinants of oligomerization of the aquaporin-4 channelen
dc.typeJournal articleen
dc.identifier.eissn1083-351X
dc.identifier.journalJournal of Biological Chemistryen
dc.date.updated2019-05-09T13:33:39Z
dc.contributor.institutionFrom the Molecular Assembly and Organisation in Cells Doctoral Training Centre, University of Warwick, Coventry CV4 7AL, the School of Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham, B4 7ET, and the Institute of Clinical Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
pubs.place-of-publicationUnited States
dc.date.accepted2016-01-15
rioxxterms.funderUniversity of Wolverhamptonen
rioxxterms.identifier.project1091578en
rioxxterms.identifier.projectBB/L502194/1en
rioxxterms.identifier.projectBB/K013319/1en
rioxxterms.identifier.projectBB/I019960/1en
rioxxterms.versionVoRen
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2019-05-13en
dc.source.volume291
dc.source.issue13
dc.source.beginpage6858
dc.source.endpage6871
dc.description.versionPublished version
refterms.dateFCD2019-05-13T10:02:58Z
refterms.versionFCDVoR
refterms.dateFOA2019-05-13T10:04:44Z


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