Journal
PLANT CELL AND ENVIRONMENT
Volume 43, Issue 10, Pages 2428-2442Publisher
WILEY
DOI: 10.1111/pce.13851
Keywords
aquaporin; Arabidopsis; gating; NSCC; osmotic stress; potassium; regulation; salt stress; sodium transport; trafficking
Categories
Funding
- Australian Research Council [DP190102725, FT180100476]
- Australian Research Council Centre of Excellence for Translational Photosynthesis [CE1401000015]
- Australian Research Council Centre of Excellence in Plant Energy Biology [CE140100008]
- Grains Research and Development Corporation [9174824]
- Australian Research Council [FT180100476] Funding Source: Australian Research Council
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The phosphorylation state of two serine residues within the C-terminal domain of AtPIP2;1 (S280, S283) regulates its plasma membrane localization 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. InXenopus laevisoocytes, 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 inSaccharomyces cerevisiaeconfirmed that phosphorylation influences plasma membrane localization, 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 localization and cation transport capacity.
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