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dc.contributor.authorQiu, J.en
dc.contributor.authorMcGaughey, S.A.en
dc.contributor.authorGroszmann, M.en
dc.contributor.authorTyerman, S.D.en
dc.contributor.authorByrt, C.S.en
dc.identifier.citationPlant, Cell & Environment, 2020; 43(10):2428-2442en
dc.descriptionFirst published: 17 July 2020en
dc.description.abstractThe phosphorylation state of two serine residues within the C-terminal domain of AtPIP2;1 (S280, S283) regulate its plasma membrane localisation in response to salt and osmotic stress. Here we investigated whether the phosphorylation state of S280 and S283 also influence AtPIP2;1 facilitated water and cation transport. A series of single and double S280 and S283 phosphomimic and phosphonull AtPIP2;1 mutants were tested in heterologous systems. In Xenopus laevis oocytes, phosphomimic mutants AtPIP2;1 S280D, S283D, and S280D/S283D had significantly greater ion conductance for Na+ and K+ , whereas the S280A single phosphonull mutant had greater water permeability. We observed a phosphorylation-dependent inverse relationship between AtPIP2;1 water and ion transport with a 10-fold change in both. The results revealed that phosphorylation of S280 and S283 influences the preferential facilitation of ion or water transport by AtPIP2;1. The results also hint that other regulatory sites play roles that are yet to be elucidated. Expression of the AtPIP2;1 phosphorylation mutants in Saccharomyces cerevisiae confirmed that phosphorylation influences plasma membrane localisation, and revealed higher Na+ accumulation for S280A and S283D mutants. Collectively, the results show that phosphorylation in the C-terminal domain of AtPIP2;1 influences its subcellular localisation and cation transport capacity. This article is protected by copyright. All rights reserved.en
dc.description.statementofresponsibilityJiaen Qiu, Samantha A. McGaughey, Michael Groszmann, Stephen D. Tyerman, Caitlin S. Byrten
dc.rights© 2020 John Wiley & Sons Ltd.en
dc.subjectArabidopsis; NSCC; aquaporin; gating; osmotic stress; potassium; regulation; salt stress; sodium transport; traffickingen
dc.titlePhosphorylation influences water and ion channel function of AtPIP2;1en
dc.typeJournal articleen
pubs.library.collectionAgriculture, Food and Wine publicationsen
dc.identifier.orcidQiu, J. [0000-0001-9220-4219]en
dc.identifier.orcidMcGaughey, S.A. [0000-0001-6133-0415]en
dc.identifier.orcidTyerman, S.D. [0000-0003-2455-1643]en
dc.identifier.orcidByrt, C.S. [0000-0001-8549-2873]en
Appears in Collections:Agriculture, Food and Wine publications

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