Abstract
Hypoxic conditions often arise from waterlogging and flooding, affecting several aspects of plant metabolism, including the uptake of nutrients. We identified a member of the CALCINEURIN β-LIKE INTERACTING PROTEIN KINASE (CIPK) family in Arabidopsis, CIPK25, which is induced in the root endodermis under low-oxygen conditions. A cipk25 mutant exhibited higher sensitivity to anoxia in conditions of potassium limitation, suggesting that this kinase is involved in the regulation of potassium uptake. Interestingly, we found that CIPK25 interacts with AKT1, the major inward rectifying potassium channel in Arabidopsis. Under anoxic conditions, cipk25 mutant seedlings were unable to maintain potassium concentrations at wild-type levels, suggesting that CIPK25 likely plays a role in modulating potassium homeostasis under low-oxygen conditions. In addition, cipk25 and akt1 mutants share similar developmental defects under waterlogging, further supporting an interplay between CIPK25 and AKT1.
Highlights
The intensification of flooding events is one of the consequences of climate change that is strongly affecting plant biodiversity and crop productivity
We identified a member of the CALCINEURIN β-LIKE INTERACTING PROTEIN KINASE (CIPK) family in Arabidopsis, CIPK25, which is induced in the root endodermis under low-oxygen conditions
Among the 26 CIPKs encoded by the Arabidopsis genome, CIPK25 (At5g25110) is transcriptionally induced under low-O2 conditions (Supplementary Fig. S1), pointing to a putative role for this kinase under this stress condition
Summary
The intensification of flooding events is one of the consequences of climate change that is strongly affecting plant biodiversity and crop productivity. Low O2 availability for plants is a consequence of environmental stress and occurs during the development of specific organs and tissues, such as fruits, root vasculature, and seeds (Van Dongen and Licausi, 2015). PCO enzymes destabilize ERF-VIIs through the O2-dependent oxidation of an N-terminal cysteine, targeting the ERF-VIIs for proteasomal degradation. This process is prevented under O2 limitation, allowing ERF-VIIs to act as transcriptional activators of genes involved in anaerobic metabolism
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