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https://hdl.handle.net/2440/127608
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DC Field | Value | Language |
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dc.contributor.author | Qiu, J. | - |
dc.contributor.author | McGaughey, S.A. | - |
dc.contributor.author | Groszmann, M. | - |
dc.contributor.author | Tyerman, S.D. | - |
dc.contributor.author | Byrt, C.S. | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | Plant, Cell and Environment, 2020; 43(10):2428-2442 | - |
dc.identifier.issn | 0140-7791 | - |
dc.identifier.issn | 1365-3040 | - |
dc.identifier.uri | http://hdl.handle.net/2440/127608 | - |
dc.description | First published: 17 July 2020 | - |
dc.description.abstract | The 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. | - |
dc.description.statementofresponsibility | Jiaen Qiu, Samantha A. McGaughey, Michael Groszmann, Stephen D. Tyerman, Caitlin S. Byrt | - |
dc.language.iso | en | - |
dc.publisher | Wiley | - |
dc.rights | © 2020 John Wiley & Sons Ltd. | - |
dc.source.uri | http://dx.doi.org/10.1111/pce.13851 | - |
dc.subject | Arabidopsis | - |
dc.subject | NSCC | - |
dc.subject | aquaporin | - |
dc.subject | gating | - |
dc.subject | osmotic stress | - |
dc.subject | potassium | - |
dc.subject | regulation | - |
dc.subject | salt stress | - |
dc.subject | sodium transport | - |
dc.subject | trafficking | - |
dc.title | Phosphorylation influences water and ion channel function of AtPIP2;1 | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1111/pce.13851 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/DP190102725 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/FT180100476 | - |
dc.relation.grant | http://purl.org/au-research/grants/arc/CE1401000015 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Qiu, J. [0000-0001-9220-4219] | - |
dc.identifier.orcid | McGaughey, S.A. [0000-0001-6133-0415] | - |
dc.identifier.orcid | Tyerman, S.D. [0000-0003-2455-1643] | - |
dc.identifier.orcid | Byrt, C.S. [0000-0001-8549-2873] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 4 |
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