Phospho-OXSR1 (T185) Antibody

1. Data demonstrate that hypotonic low-chloride conditions that activate the WNK1-SPAK and OSR1 pathway promote phosphorylation of NKCC2 isoforms. PMID: 21321328
2. OSR1 and SPAK integrate signals from osmosensing and survival pathways. PMID: 24191005
3. our data show a novel role for the WNK1/OSR1/NKCC1 pathway in glioma migration PMID: 24555568
4. SPAK and OSR1 are powerful negative regulators of the cell volume regulatory Cl- channel ClC-2 PMID: 25323061
5. study identifies a separation of functions for the WNK1-activated protein kinases OSR1 and SPAK in mediating proliferation, invasion, and gene expression in endothelial cells PMID: 25362046
6. The CCT domain directly interacts with the kinase domain to block substrate access and inhibit the domain-swapped homodimerization of the kinase domain of OSR1. PMID: 25389294
7. WNK 1, 3, 4, OSR1, and SPAK signaling system known to play a role in regulating the phosphorylation status, and hence activity of the CCCs in other tissues, is also present in the rat and human lenses. PMID: 25515571
8. OSR1 has the capacity to downregulate the peptide transporters PEPT1 and PEPT2 by decreasing the carrier protein abundance in the cell membrane PMID: 25531100
9. Both, SPAK and OSR1, are negative regulators of the creatine transporter SLC6A8 PMID: 25531585
10. SPAK and OSR1 are negative regulators of EAAT3 activity PMID: 26112741
11. SPAK and OSR1 are powerful negative regulators of the excitatory glutamate transporters EAAT1 and EAAT2. PMID: 26233565
12. SPAK and OSR1 are powerful stimulators of the intestinal Na+-coupled phosphate co-transporter NaPi-IIb PMID: 26506223
13. OSR1 protein has both the potential to up-regulate KCNQ1/E1 protein abundance in the cell membrane, an effect possibly participating in the regulation of cell volume, excitability, epithelial transport and metabolism. PMID: 26584301
14. SPAK and OSR1 are both stimulators of Kir2.1 activity. PMID: 26673921
15. Both SPAK and OSR1 kinases entering cells through exosomes are preferentially expressed at the plasma membrane and that the kinases in exosomes are functional and maintain NKCC1 in a phosphorylated state. PMID: 27122160
16. the WNK-regulated SPAK/OSR1 kinases directly phosphorylate the N[K]CCs and KCCs, promoting their stimulation and inhibition respectively. PMID: 24393035
17. SPAK and OSR1, which are often coexpressed in cells, can form functional heterodimers. PMID: 23034389
18. Data show that intracellular association between WNK1 and oxidative stress-responsive 1 (OSR1) is required for stimulation of OSR1 and Na(+), K(+), Cl(-)-Cotransporter NKCC1 and NKCC2 activities by osmotic stress. PMID: 22989884
19. OXSR1 and WNK3 transcripts were substantially overexpressed in subjects with schizophrenia relative to comparison subjects. PMID: 20819979
20. interacts with cation chloride cotransporters PMID: 12386165
21. isolation and characterization of OSR1 (oxidative stress-responsive 1), one of two human Fray homologs. OSR1 is a 58-kDa protein of 527 amino acids that is widely expressed in mammalian tissues and cell lines PMID: 14707132
22. WNK1 and SPAK/OSR1 mediate the hypotonic stress signaling pathway to cation-chloride-coupled cotransporters PMID: 16263722
23. OXSR1 kinase is shown to interact with the three RELT family members RELT, RELL1, and RELL2 by in vitro co-immunoprecipitation; additionally, OXSR1 phosphorylates RELT family members in an in vitro kinase assay. PMID: 16389068
24. data establish that the CCT domain functions as a multipurpose docking site, enabling SPAK/OSR1 to interact with substrates (NKCC1) and activators (WNK1/WNK4) PMID: 16669787
25. OSR1 and sterile20-related, proline-, alanine-rich kinase are likely links between WNK lysine deficient protein kinase 1 and solute carrier family 12 in a pathway that contributes to volume regulation and blood pressure homeostasis in mammals PMID: 16832045
26. These results provide the first molecular insight into the mechanism by which the SPAK and OSR1 kinases specifically recognize their upstream activators and downstream substrates. PMID: 17721439
27. The WNK1-SPAK/OSR1 signalling pathway plays a key role in controlling the phosphorylation and activity of NCC. PMID: 18270262
28. The first crystal structure of an OSR1 fragment encompassing the catalytic domain of the enzyme, is reported. PMID: 18831043
29. crystal structure of OSR1 kinase domain has been solved at 2.25 A; OSR1 forms a domain-swapped dimer in an inactive conformation, in which P+1 loop and alphaEF helix are swapped between dimer-related monomers PMID: 19177573

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HGNC: 8508

OMIM: 604046

KEGG: hsa:9943

STRING: 9606.ENSP00000311713

UniGene: Hs.475970