Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/127608
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: Phosphorylation influences water and ion channel function of AtPIP2;1
Author: Qiu, J.
McGaughey, S.A.
Groszmann, M.
Tyerman, S.D.
Byrt, C.S.
Citation: Plant, Cell & Environment, 2020; 43(10):2428-2442
Publisher: Wiley
Issue Date: 2020
ISSN: 0140-7791
1365-3040
Statement of
Responsibility: 
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.
RMID: 1000023824
DOI: 10.1111/pce.13851
Grant ID: http://purl.org/au-research/grants/arc/DP190102725
http://purl.org/au-research/grants/arc/FT180100476
http://purl.org/au-research/grants/arc/CE1401000015
Appears in Collections:Agriculture, Food and Wine publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.