{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Li KL"],"pubmed_abstract":["Under low-potassium (K<sup>+</sup>) stress, a Ca<sup>2+</sup> 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<sup>+</sup> uptake and remobilization, respectively, by activating a series of K<sup>+</sup> channels. While the dual CBL-CIPK pathways enable plants to cope with low-K<sup>+</sup> stress, little is known about the early events that link external K<sup>+</sup> levels to the CBL-CIPK proteins. Here we show that K<sup>+</sup> status regulates the protein abundance and phosphorylation of the CBL-CIPK-channel modules. Further analysis revealed low K<sup>+</sup>-induced activation of VM-CBL2/3 happened earlier"],"journal":["Nature communications"],"pagination":["360"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9870859"],"repository":["biostudies-literature"],"pubmed_title":["Potassium nutrient status drives posttranslational regulation of a low-K response network in Arabidopsis."],"pmcid":["PMC9870859"],"pubmed_authors":["Wang C","Luan S","Li KL","Tang RJ"],"additional_accession":[]},"is_claimable":false,"name":"Potassium nutrient status drives posttranslational regulation of a low-K response network in Arabidopsis.","description":"Under low-potassium (K<sup>+</sup>) stress, a Ca<sup>2+</sup> 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<sup>+</sup> uptake and remobilization, respectively, by activating a series of K<sup>+</sup> channels. While the dual CBL-CIPK pathways enable plants to cope with low-K<sup>+</sup> stress, little is known about the early events that link external K<sup>+</sup> levels to the CBL-CIPK proteins. Here we show that K<sup>+</sup> status regulates the protein abundance and phosphorylation of the CBL-CIPK-channel modules. Further analysis revealed low K<sup>+</sup>-induced activation of VM-CBL2/3 happened earlier","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2025-04-18T18:18:08.081Z","creation":"2025-04-07T05:55:31.003Z"},"accession":"S-EPMC9870859","cross_references":{"pubmed":["36690625"],"doi":["10.1038/s41467-023-35906-5"]}}