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|Title:||Phosphorylation influences water and ion channel function of AtPIP2;1|
|Citation:||Plant, Cell & Environment, 2020; 43(10):2428-2442|
|Jiaen Qiu, Samantha A. McGaughey, Michael Groszmann, Stephen D. Tyerman, Caitlin S. Byrt|
|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.|
|Keywords:||Arabidopsis; NSCC; aquaporin; gating; osmotic stress; potassium; regulation; salt stress; sodium transport; trafficking|
|Description:||First published: 17 July 2020|
|Rights:||© 2020 John Wiley & Sons Ltd.|
|Appears in Collections:||Agriculture, Food and Wine publications|
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