Ask about this productRelated genes to: OXSR1 antibody
- Gene:
- OXSR1 NIH gene
- Name:
- oxidative stress responsive kinase 1
- Previous symbol:
- OSR1
- Synonyms:
- KIAA1101
- Chromosome:
- 3p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-06
- Date modifiied:
- 2018-10-15
Related products to: OXSR1 antibody
Related articles to: OXSR1 antibody
- - Source: PubMed
Publication date: 2026/04/23
- Animals activate regenerative processes to repair injuries and restore homeostasis following tissue damage. A central question in regeneration is how damage signals are sensed and translated into regenerative growth. Tissue injuries lead to the release of intracellular contents and bodily fluids and disturb the osmotic balance. However, the role of osmolarity in regeneration remains largely unexplored. Using Drosophila and mouse intestine, as well as samples from inflammatory bowel disease (IBD) patients, we identify a key role for the osmolarity-sensing WNK-OXSR1 kinase cascade in intestinal regeneration. Mechanistically, OXSR1 phosphorylates the RhoB GTPase at threonine 37 upon intestinal injury, thereby disrupting its interaction with ARHGAP17 and increasing the levels of GTP-bound RhoB. RhoB activation in turn leads to enhanced F-actin polymerization and YAP activation, thus promoting tissue regeneration. We further show that pharmacological inhibition of WNK or OXSR1 reduces the oncogenic potential of intestinal regeneration. These findings reveal osmolarity as a critical damage signal in regeneration and position WNK-OXSR1 as a potential therapeutic target for stimulating intestinal repair. - Source: PubMed
Publication date: 2026/03/18
Cao HemingHuang XiaweiJiang XiaobingDeng JingrongWang JiahuiWu ChengfangHu MinhuangZeng BeiHu ZhihaoPan HuiminYang YuxiaZheng KeweiShen RuiZhang MingqingLiu Bo - Life depends on maintaining water homeostasis and internal osmolality constancy. In terrestrial animals, the release of the antidiuretic hormone arginine vasopressin (AVP) in response to variations of extracellular osmolality (tonicity) is crucial. We have reported that WNK1 kinase in the vascular-organ-of-lamina-terminalis (OVLT) nuclei of the brain mediates the hypertonicity-induced AVP release by activating the voltage-gated K channel Kv3.1 increasing action potential firing. The downstream mechanism for WNK1-mediated osmosensation is unknown. Here, we showed that the hypertonicity-induced increases in Kv3.1 currents in cultured cells required the oxidative stress-responsive-1 (OSR1) or STE20/SPS1-related proline/alanine-rich (SPAK) kinase. Both kinases were present in the mouse OVLT area. Hypertonicity induced by water restriction or mannitol injection increased the abundance of phosphorylated OSR1 and SPAK in the OVLT. Double deletion of Osr1 and Spak in the OVLT in mice caused polyuria with relative hypotonic urine that persisted in water restriction. The water restriction-induced AVP release was blunted in Osr1 and Spak-deleted mice. In brain slice recordings, the hypertonicity-induced increases in action potential firing in OVLT were blunted by Osr1 and Spak deletion. Deletion of the Kv3.1 channel in the OVLT showed a similar phenotype. Expression of the constitutively active OSR1 in the OVLT resulted in increased AVP release and inappropriate antidiuretic hormone secretion phenotype. In summary, OSR1/SPAK acts downstream of WNK1 to regulate AVP release in response to hypertonicity. In OVLT neurons OSR1/SPAK activates Kv3.1 to increase action potential firing. Thus, the WNK1-OSR1/SPAK-Kv3.1 cascade regulates water homeostasis and AVP release to control osmolality stability. - Source: PubMed
Jin XinXie JianYeh Chia-WeiLi Yu-JuiLien Cheng-ChangHuang Chou-Long - Aortic stenosis (AS) is a prevalent valvular heart disease that is increasing due to aging population and longer life expectancy. While most individuals have a tricuspid aortic valve (TAV), some are congenitally born with a bicuspid aortic valve (BAV). The mechanisms underlying AS pathogenesis remain unclear, limiting advancements in clinical treatment and biomedical research. This study aimed to identify differentially expressed protein (DEPs) in aortic valve interstitial cells (VICs) from AS patients with TAV and BAV using quantitative proteomic analysis. - Source: PubMed
Publication date: 2025/09/01
Song NaaleumYu JiyoungJi EunhyeYoon JinChoi Kyoung-HeeYu Jeong EunKim BokyungKim JihyeonKim MinjoongLee SahminKim KyunggonAikawa Elena - The WNK-OSR1/SPAK protein kinase pathway regulates ion homeostasis and cell volume, but its other functions are not well understood. To discover undefined signaling functions, we utilized experimentally-derived binding specificity to predict interactions and relative affinities with the conserved C-terminal (CCT) domains of OSR1 and SPAK, which bind short linear motifs. The upstream kinases WNKs 1-4 and their relatives, the pseudokinases NRBP1/2, also contain CCT-like domains which have conserved folds and motif binding pockets. Motifs were scored using peptide arrays, conservation, cytosolic localization, and solvent accessibility. Out of nearly 3700 motifs in the human proteome, 90% of previously published motifs ranked in the top 2% of those predicted. Interactions with selected candidates, including TSC22D1 and CAVIN1, were validated, and their localization and/or modifications were coupled to changes in WNK1 signaling. We also identified additional motif variants and confirmed binding to the NRBP1 CCT-like domain. Our results stress the diverse functionality of CCT/CCT-like domains and implicates unexpected interactions driving WNK biology. - Source: PubMed
Publication date: 2025/09/05
Taylor Clinton AJung Ji-UngGallolu Kankanamalage SachithLi JustinGrzemska MagdalenaJaykumar Ankita BEarnest SvetlanaStippec SteveSaha PurbitaSauceda EustoliaCobb Melanie H