biostudies-literatureUnknown14(1)Li KLUnder low-potassium (K⁺) stress, a Ca²⁺ signaling network consisting of calcineurin B-like proteins (CBLs) and CBL-interacting kinases (CIPKs) play essential roles. Specifically, the plasma membrane CBL1/9-CIPK pathway and the tonoplast CBL2/3-CIPK pathway promotes K⁺ uptake and remobilization, respectively, by activating a series of K⁺ channels. While the dual CBL-CIPK pathways enable plants to cope with low-K⁺ stress, little is known about the early events that link external K⁺ levels to the CBL-CIPK proteins. Here we show that K⁺ status regulates the protein abundance and phosphorylation of the CBL-CIPK-channel modules. Further analysis revealed low K⁺-induced activation of VM-CBL2/3 happened earlierNature communications360https://www.ebi.ac.uk/biostudies/studies/S-EPMC9870859biostudies-literaturePotassium nutrient status drives posttranslational regulation of a low-K response network in Arabidopsis.PMC9870859Wang CLuan SLi KLTang RJfalsePotassium nutrient status drives posttranslational regulation of a low-K response network in Arabidopsis.Under low-potassium (K⁺) stress, a Ca²⁺ signaling network consisting of calcineurin B-like proteins (CBLs) and CBL-interacting kinases (CIPKs) play essential roles. Specifically, the plasma membrane CBL1/9-CIPK pathway and the tonoplast CBL2/3-CIPK pathway promotes K⁺ uptake and remobilization, respectively, by activating a series of K⁺ channels. While the dual CBL-CIPK pathways enable plants to cope with low-K⁺ stress, little is known about the early events that link external K⁺ levels to the CBL-CIPK proteins. Here we show that K⁺ status regulates the protein abundance and phosphorylation of the CBL-CIPK-channel modules. Further analysis revealed low K⁺-induced activation of VM-CBL2/3 happened earlier2023-01-01T00:00:00Z2023 Jan2025-04-18T18:18:08.081Z2025-04-07T05:55:31.003ZS-EPMC98708593669062510.1038/s41467-023-35906-5