{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOxidative stress‐responsive kinase 1 (OXSR1, also known as OSR1) is a serine/threonine protein kinase that lies at the heart of a signaling cascade linking the with‐no‐lysine (WNK) kinases to the regulation of ion transport. It is activated by WNK1/4 under osmotic and oxidative stress conditions and, in turn, phosphorylates and modulates key cation–chloride cotransporters such as NKCC1, NKCC2, and NCC, while also inhibiting KCCs. Structural studies have revealed that OSR1 contains a highly conserved C-terminal (CCT) docking domain that mediates its interactions with upstream WNK kinases and substrates, and its activity is regulated by a complex “double lock” autoinhibitory mechanism. These features underpin its critical roles in maintaining cell volume and ion homeostasis in diverse tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in ion regulation, OSR1 is intimately involved in integrated cellular signaling pathways that impact diverse functions. For instance, OSR1 can phosphorylate downstream targets involved in stress responses, cytoskeletal regulation, and cell survival – including modulation of neurotransmitter transporter activity (affecting GABAergic and glutamatergic signaling) and channel function in epithelial and neural cells. OSR1 also contributes to vascular development, as demonstrated by its ability to rescue angiogenic defects in WNK1-deficient endothelial cells, and it has been implicated in the regulation of specialized transport processes such as lens transparency, peptide uptake, and the function of excitatory amino acid transporters. Furthermore, interactions with partners like PAK1 and involvement in multimeric complexes (for example, via domain swapping in kinase concatemers) highlight a sophisticated network by which OSR1 orchestrates cellular responses to osmotic stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinical and translational studies further underscore the importance of OSR1 in human disease. Altered OSR1 expression and activity are linked with hypertension and disorders of renal ion transport (as in autosomal-dominant polycystic kidney disease), while its interactions with membrane receptors such as the β₂-adrenergic receptor and potential presence in exosomes hint at broader roles in cell signaling and intercellular communication. Moreover, emerging evidence suggests that genetic variation in OXSR1 may influence the risk or severity of conditions such as breast cancer and asthma, and structure-guided efforts aimed at inhibiting its docking interactions present promising avenues for novel therapeutic strategies in hypertension and ischemic stroke."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "26", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kerstin Piechotta, Jianming Lu, Eric Delpire "}, {"type": "b", "children": [{"type": "t", "text": "Cation chloride cotransporters interact with the stress-related kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress response 1 (OSR1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M208108200"}], "href": "https://doi.org/10.1074/jbc.M208108200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12386165"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12386165"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Tetsuo Moriguchi, Seiichi Urushiyama, Naoki Hisamoto, et al. 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