Abstract
In plants, aquaporins play a crucial role in regulating root water transport in response to environmental and physiological cues. Controls achieved at the post-translational level are thought to be of critical importance for regulating aquaporin function. To investigate the general molecular mechanisms involved, we performed, using the model species Arabidopsis, a comprehensive proteomic analysis of root aquaporins in a large set of physiological contexts. We identified nine physiological treatments that modulate root hydraulics in time frames of minutes (NO and H2O2 treatments), hours (mannitol and NaCl treatments, exposure to darkness and reversal with sucrose, phosphate supply to phosphate-starved roots), or days (phosphate or nitrogen starvation). All treatments induced inhibition of root water transport except for sucrose supply to dark-grown plants and phosphate resupply to phosphate-starved plants, which had opposing effects. Using a robust label-free quantitative proteomic methodology, we identified 12 of 13 plasma membrane intrinsic protein (PIP) aquaporin isoforms, 4 of the 10 tonoplast intrinsic protein isoforms, and a diversity of post-translational modifications including phosphorylation, methylation, deamidation, and acetylation. A total of 55 aquaporin peptides displayed significant changes after treatments and enabled the identification of specific and as yet unknown patterns of response to stimuli. The data show that the regulation of PIP and tonoplast intrinsic protein abundance was involved in response to a few treatments (i.e. NaCl, NO, and nitrate starvation), whereas changes in the phosphorylation status of PIP aquaporins were positively correlated to changes in root hydraulic conductivity in the whole set of treatments. The identification of in vivo deamidated forms of aquaporins and their stimulus-induced changes in abundance may reflect a new mechanism of aquaporin regulation. The overall work provides deep insights into the in vivo post-translational events triggered by environmental constraints and their possible role in regulating plant water status.
Highlights
To cite this version: Magali Di Pietro, Jérôme Vialaret, Guo-Wei Li, Sonia Hem, Karine Prado, et al
The data show that the regulation of plasma membrane intrinsic protein (PIP) and tonoplast intrinsic protein abundance was involved in response to a few treatments (i.e. NaCl, Nitric oxide (NO), and nitrate starvation), whereas changes in the phosphorylation status of PIP aquaporins were positively correlated to changes in root hydraulic conductivity in the whole set of treatments
Modulation of Lpr by Multiple Abiotic Treatments—In a previous study, we showed that exposure of Arabidopsis roots to 100 mM NaCl induces a rapid and marked (Ϫ70%) decrease in Lpr [22]
Summary
To cite this version: Magali Di Pietro, Jérôme Vialaret, Guo-Wei Li, Sonia Hem, Karine Prado, et al. Aquaporins play a crucial role in regulating root water transport in response to environmental and physiological cues. To investigate the general molecular mechanisms involved, we performed, using the model species Arabidopsis, a comprehensive proteomic analysis of root aquaporins in a large set of physiological contexts. Using a robust label-free quantitative proteomic methodology, we identified 12 of 13 plasma membrane intrinsic protein (PIP) aquaporin isoforms, 4 of the 10 tonoplast intrinsic protein isoforms, and a diversity of post-translational modifications including phosphorylation, methylation, deamidation, and acetylation. The data show that the regulation of PIP and tonoplast intrinsic protein abundance was involved in response to a few treatments (i.e. NaCl, NO, and nitrate starvation), whereas changes in the phosphorylation status of PIP aquaporins were positively correlated to changes in root hydraulic conductivity in the whole set of treatments. From ‡Biochimie et Physiologie Moleculaire des Plantes, SupAgro/ INRA/CNRS/UMII/UMR 5004, 2 Place Viala, 34060 F-Montpellier cedex 1, France; ¶Laboratoire de Proteomique Fonctionnelle, UR 1199, 1 Place Viala, 34060 F-Montpellier Cedex 1, France
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