Structural determinants of oligomerization of the aquaporin-4 channel
dc.contributor.author | Kitchen, P | |
dc.contributor.author | Conner, MT | |
dc.contributor.author | Bill, RM | |
dc.contributor.author | Conner, AC | |
dc.date.accessioned | 2019-05-13T10:04:43Z | |
dc.date.available | 2019-05-13T10:04:43Z | |
dc.date.issued | 2016-01-19 | |
dc.identifier.citation | Kitchen, 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.issn | 0021-9258 | en |
dc.identifier.pmid | 26786101 | |
dc.identifier.doi | 10.1074/jbc.M115.694729 | en |
dc.identifier.uri | http://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.sponsorship | Supported 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.format | application/PDF | en |
dc.language | eng | |
dc.language.iso | en | en |
dc.publisher | American Society for Biochemistry & Molecular Biology (ASBMB) | en |
dc.relation.url | http://www.jbc.org/content/291/13/6858 | en |
dc.rights | Licence for published version: Creative Commons Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.subject | Animals | en |
dc.subject | Dogs | en |
dc.subject | Humans | en |
dc.subject | Escherichia coli | en |
dc.subject | Water | en |
dc.subject | Recombinant Proteins | en |
dc.subject | Crystallography, X-Ray | en |
dc.subject | Cloning, Molecular | en |
dc.subject | Sequence Alignment | en |
dc.subject | Gene Expression | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Protein Structure, Secondary | en |
dc.subject | Structural Homology, Protein | en |
dc.subject | Protein Transport | en |
dc.subject | Mutation | en |
dc.subject | Hydrogen Bonding | en |
dc.subject | Osmolar Concentration | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | Aquaporin 1 | en |
dc.subject | Aquaporin 3 | en |
dc.subject | Aquaporin 4 | en |
dc.subject | Protein Interaction Domains and Motifs | en |
dc.subject | Protein Multimerization | en |
dc.subject | Molecular Dynamics Simulation | en |
dc.subject | HEK293 Cells | en |
dc.subject | Madin Darby Canine Kidney Cells | en |
dc.title | Structural determinants of oligomerization of the aquaporin-4 channel | en |
dc.type | Journal article | en |
dc.identifier.eissn | 1083-351X | |
dc.identifier.journal | Journal of Biological Chemistry | en |
dc.date.updated | 2019-05-09T13:33:39Z | |
dc.contributor.institution | From 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-publication | United States | |
dc.date.accepted | 2016-01-15 | |
rioxxterms.funder | University of Wolverhampton | en |
rioxxterms.identifier.project | 1091578 | en |
rioxxterms.identifier.project | BB/L502194/1 | en |
rioxxterms.identifier.project | BB/K013319/1 | en |
rioxxterms.identifier.project | BB/I019960/1 | en |
rioxxterms.version | VoR | en |
rioxxterms.licenseref.uri | http://creativecommons.org/licenses/by/4.0/ | en |
rioxxterms.licenseref.startdate | 2019-05-13 | en |
dc.source.volume | 291 | |
dc.source.issue | 13 | |
dc.source.beginpage | 6858 | |
dc.source.endpage | 6871 | |
dc.description.version | Published version | |
refterms.dateFCD | 2019-05-13T10:02:58Z | |
refterms.versionFCD | VoR | |
refterms.dateFOA | 2019-05-13T10:04:44Z |