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Gene Review

OXSR1  -  oxidative stress responsive 1

Homo sapiens

Synonyms: KIAA1101, OSR1, Oxidative stress-responsive 1 protein, Serine/threonine-protein kinase OSR1
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Disease relevance of OXSR1


High impact information on OXSR1


Chemical compound and disease context of OXSR1


Biological context of OXSR1

  • The residues on NKCC1, phosphorylated by SPAK/OSR1, are conserved in other cation co-transporters, such as the Na+-Cl- co-transporter, the target of thiazide drugs that lower blood pressure in humans with Gordon's syndrome [7].
  • Genetic analysis suggests that OSR1 evolved first, with SPAK arising following a gene duplication in vertebrate evolution [8].
  • SPAK and OSR1 are two recently discovered kinases which have been linked to several key cellular processes, including cell differentiation, cell transformation and proliferation, cytoskeleton rearrangement, and most recently, regulation of ion transporters [8].
  • Based on the alignment of 12 sequences of protein motifs that interact with the kinases SPAK (Ste20-related proline alanine-rich kinase) and OSR1 (oxidative stress response 1), we performed genome-wide searches of the sequence [S/G/V]RFx[V/I]xx[V/I/T/S]xx, where x represents any amino acid [9].
  • Taken together, we propose that human Ngb may be a novel oxidative stress-responsive sensor for signal transduction in the brain [10].

Anatomical context of OXSR1


Associations of OXSR1 with chemical compounds


Regulatory relationships of OXSR1

  • We have identified specific residues within the CCT domain that are required for interaction with the RFXV motif and have demonstrated that mutation of these in OSR1 inhibited phosphorylation of NKCC1, but not of CATCHtide which does not possess an RFXV motif [7].

Other interactions of OXSR1


Analytical, diagnostic and therapeutic context of OXSR1


  1. Oxidative stress-responsive transcription factor ATF3 potentially mediates diabetic angiopathy. Okamoto, A., Iwamoto, Y., Maru, Y. Mol. Cell. Biol. (2006) [Pubmed]
  2. WNK1 and OSR1 regulate the Na+, K+, 2Cl- cotransporter in HeLa cells. Anselmo, A.N., Earnest, S., Chen, W., Juang, Y.C., Kim, S.C., Zhao, Y., Cobb, M.H. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Oxidative stress induces NF-kappaB nuclear translocation without degradation of IkappaBalpha. Canty, T.G., Boyle, E.M., Farr, A., Morgan, E.N., Verrier, E.D., Pohlman, T.H. Circulation (1999) [Pubmed]
  4. WNK1 regulates phosphorylation of cation-chloride-coupled cotransporters via the STE20-related kinases, SPAK and OSR1. Moriguchi, T., Urushiyama, S., Hisamoto, N., Iemura, S., Uchida, S., Natsume, T., Matsumoto, K., Shibuya, H. J. Biol. Chem. (2005) [Pubmed]
  5. Characterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamily. Chen, W., Yazicioglu, M., Cobb, M.H. J. Biol. Chem. (2004) [Pubmed]
  6. Effects of flavonoids on the expression of the pro-inflammatory response in human monocytes induced by ligation of the receptor for AGEs. Huang, S.M., Wu, C.H., Yen, G.C. Molecular nutrition & food research (2006) [Pubmed]
  7. Functional interactions of the SPAK/OSR1 kinases with their upstream activator WNK1 and downstream substrate NKCC1. Vitari, A.C., Thastrup, J., Rafiqi, F.H., Deak, M., Morrice, N.A., Karlsson, H.K., Alessi, D.R. Biochem. J. (2006) [Pubmed]
  8. SPAK and OSR1, key kinases involved in the regulation of chloride transport. Delpire, E., Gagnon, K.B. Acta physiologica (Oxford, England) (2006) [Pubmed]
  9. Genome-wide analysis of SPAK/OSR1 binding motifs. Delpire, E., Gagnon, K.B. Physiol. Genomics (2007) [Pubmed]
  10. Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor. Wakasugi, K., Nakano, T., Morishima, I. J. Biol. Chem. (2003) [Pubmed]
  11. Hypotonic shock mediation by p38 MAPK, JNK, PKC, FAK, OSR1 and SPAK in osmosensing chloride secreting cells of killifish opercular epithelium. Marshall, W.S., Ossum, C.G., Hoffmann, E.K. J. Exp. Biol. (2005) [Pubmed]
  12. Nutritional implications in vascular endothelial cell metabolism. Hennig, B., Toborek, M., McClain, C.J., Diana, J.N. Journal of the American College of Nutrition. (1996) [Pubmed]
  13. Reversible hexa- to penta-coordination of the heme Fe atom modulates ligand binding properties of neuroglobin and cytoglobin. Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., Burmester, T., Ascenzi, P., Bolognesi, M. IUBMB Life (2004) [Pubmed]
  14. The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases. Vitari, A.C., Deak, M., Morrice, N.A., Alessi, D.R. Biochem. J. (2005) [Pubmed]
  15. Cation chloride cotransporters interact with the stress-related kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative stress response 1 (OSR1). Piechotta, K., Lu, J., Delpire, E. J. Biol. Chem. (2002) [Pubmed]
  16. Multiple oxidative stress-response members of the Adapt78 family. Michtalik, H.J., Narayan, A.V., Bhatt, N., Lin, H.Y., Mulligan, M.T., Zhang, S.L., Crawford, D.R. Free Radic. Biol. Med. (2004) [Pubmed]
  17. Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase. Wakasugi, K., Nakano, T., Morishima, I. Biochemistry (2005) [Pubmed]
  18. Buffering capacity of coal and its acid-soluble Fe2+ content: possible role in coal workers' pneumoconiosis. Huang, X., Fournier, J., Koenig, K., Chen, L.C. Chem. Res. Toxicol. (1998) [Pubmed]
  19. Redox-sensitive mechanisms of phytochemical-mediated inhibition of cancer cell proliferation (review). Loo, G. J. Nutr. Biochem. (2003) [Pubmed]
  20. Influence of nutrients and cytokines on endothelial cell metabolism. Hennig, B., Diana, J.N., Toborek, M., McClain, C.J. Journal of the American College of Nutrition. (1994) [Pubmed]
  21. Identification of RELT homologues that associate with RELT and are phosphorylated by OSR1. Cusick, J.K., Xu, L.G., Bin, L.H., Han, K.J., Shu, H.B. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  22. The role of oxidative stress in zearalenone-mediated toxicity in Hep G2 cells: Oxidative DNA damage, gluthatione depletion and stress proteins induction. Hassen, W., Ayed-Boussema, I., Oscoz, A.A., De Cerain Lopez, A., Bacha, H. Toxicology (2007) [Pubmed]
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