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Gene Review

Rps6ka3  -  ribosomal protein S6 kinase polypeptide 3

Mus musculus

Synonyms: 90 kDa ribosomal protein S6 kinase 3, C130006E23, MAP kinase-activated protein kinase 1b, MAPK-activated protein kinase 1b, MAPKAP kinase 1b, ...
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Disease relevance of Rps6ka3


Psychiatry related information on Rps6ka3


High impact information on Rps6ka3


Biological context of Rps6ka3

  • However, cells deficient in p90 ribosomal S6 kinase 2 (Rsk2(-/-)) totally block this phosphorylation in a dose- and time-dependent manner [7].
  • Moreover, this interaction leads to maintenance of the sustained activation of RSK2 in G1 phase of the cell cycle [8].
  • We identify the transcription factor ATF4 as a critical substrate of RSK2 that is required for the timely onset of osteoblast differentiation, for terminal differentiation of osteoblasts, and for osteoblast-specific gene expression [5].
  • The injection of constitutively active mutant forms of Rsk1 and Rsk2 does not induce a cell cycle arrest in two-cell mouse embryos [9].
  • The lined deletion contains less than approximately 0.7 cM of genetic material and includes the growth factor-regulated protein kinase gene, Rsk2 [10].

Anatomical context of Rps6ka3


Associations of Rps6ka3 with chemical compounds

  • By using purified proteins, FGF-2 is shown to directly interact through two separate domains with two RSK2 domains on both sides of the hydrophobic motif, namely the NH2-terminal kinase domain (residues 360-381) by amino acid Ser-117 and the COOH-terminal kinase domain (residues 388-400) by amino acids Leu-127 and Lys-128 [8].
  • This defect is probably not mediated by RSK2-dependent phosphorylation of c-Fos on serine 362 in the C-terminus [2].
  • Salicylic acid and aspirin inhibit the activity of RSK2 kinase and repress RSK2-dependent transcription of cyclic AMP response element binding protein- and NF-kappa B-responsive genes [13].
  • 90-kDa ribosomal S6 kinase-2 (RSK2) belongs to a family of growth factor-activated serine/threonine kinases composed of two kinase domains connected by a regulatory linker region [14].
  • RSK2-PDZ domain interactions are functionally important for synaptic transmission because neurons expressing kinase-dead RSK2 display a dramatic reduction in frequency of AMPA-type glutamate receptor-mediated miniature excitatory postsynaptic currents, an effect dependent on the PDZ ligand [15].

Enzymatic interactions of Rps6ka3

  • Furthermore, assays with Rsk-2 showed that this kinase phosphorylates H2B but not H3 in vitro [16].

Regulatory relationships of Rps6ka3


Other interactions of Rps6ka3

  • Furthermore, RSK2 is not required for activation of muscle glycogen synthase by insulin but may indirectly modulate muscle glycogen synthase activity and/or glycogen content by other mechanisms, possibly through regulation of Akt [1].
  • In the present study, we show that VV infection provoked a sustained activation of both ERK1/2 and RSK2 (ribosomal S6 kinase 2) [18].
  • Rsk-2-deficient (knockout or KO) cell lines have no detectable Rsk-2 protein, whereas Rsk-1 expression is unaltered as compared with cell lines derived from wild-type control mice [11].
  • Phosphorylation of histone H3 at serine 10 was shown to be mediated by RSK2, mitogen- and stress-activated protein kinase-1 (MSK1), and mitogen-activated protein kinases depending on the specific stimulation or stress [19].
  • Activation is classically brought about by signaling-dependent phosphorylation of a key acceptor site (Ser133 in CREB) by a number of possible kinases, including PKA, CamKIV, and Rsk-2 [20].


  1. Altered extracellular signal-regulated kinase signaling and glycogen metabolism in skeletal muscle from p90 ribosomal S6 kinase 2 knockout mice. Dufresne, S.D., Bjørbaek, C., El-Haschimi, K., Zhao, Y., Aschenbach, W.G., Moller, D.E., Goodyear, L.J. Mol. Cell. Biol. (2001) [Pubmed]
  2. Essential role of RSK2 in c-Fos-dependent osteosarcoma development. David, J.P., Mehic, D., Bakiri, L., Schilling, A.F., Mandic, V., Priemel, M., Idarraga, M.H., Reschke, M.O., Hoffmann, O., Amling, M., Wagner, E.F. J. Clin. Invest. (2005) [Pubmed]
  3. Insulin resistance and lipodystrophy in mice lacking ribosomal S6 kinase 2. El-Haschimi, K., Dufresne, S.D., Hirshman, M.F., Flier, J.S., Goodyear, L.J., Bjørbaek, C. Diabetes (2003) [Pubmed]
  4. p90 ribosomal S6 kinase 2 exerts a tonic brake on G protein-coupled receptor signaling. Sheffler, D.J., Kroeze, W.K., Garcia, B.G., Deutch, A.Y., Hufeisen, S.J., Leahy, P., Brüning, J.C., Roth, B.L. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry Syndrome. Yang, X., Matsuda, K., Bialek, P., Jacquot, S., Masuoka, H.C., Schinke, T., Li, L., Brancorsini, S., Sassone-Corsi, P., Townes, T.M., Hanauer, A., Karsenty, G. Cell (2004) [Pubmed]
  6. Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3. Sassone-Corsi, P., Mizzen, C.A., Cheung, P., Crosio, C., Monaco, L., Jacquot, S., Hanauer, A., Allis, C.D. Science (1999) [Pubmed]
  7. Arsenite-induced phosphorylation of histone H3 at serine 10 is mediated by Akt1, extracellular signal-regulated kinase 2, and p90 ribosomal S6 kinase 2 but not mitogen- and stress-activated protein kinase 1. He, Z., Ma, W.Y., Liu, G., Zhang, Y., Bode, A.M., Dong, Z. J. Biol. Chem. (2003) [Pubmed]
  8. Exogenously added fibroblast growth factor 2 (FGF-2) to NIH3T3 cells interacts with nuclear ribosomal S6 kinase 2 (RSK2) in a cell cycle-dependent manner. Soulet, F., Bailly, K., Roga, S., Lavigne, A.C., Amalric, F., Bouche, G. J. Biol. Chem. (2005) [Pubmed]
  9. p90Rsk is not involved in cytostatic factor arrest in mouse oocytes. Dumont, J., Umbhauer, M., Rassinier, P., Hanauer, A., Verlhac, M.H. J. Cell Biol. (2005) [Pubmed]
  10. Mouse mutants carrying deletions that remove the genes mutated in Coffin-Lowry syndrome and lactic acidosis. Blair, H.J., Gormally, E., Uwechue, I.C., Boyd, Y. Hum. Mol. Genet. (1998) [Pubmed]
  11. Ribosomal subunit kinase-2 is required for growth factor-stimulated transcription of the c-Fos gene. Bruning, J.C., Gillette, J.A., Zhao, Y., Bjorbaeck, C., Kotzka, J., Knebel, B., Avci, H., Hanstein, B., Lingohr, P., Moller, D.E., Krone, W., Kahn, C.R., Muller-Wieland, D. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  12. Expression pattern of the Rsk2, Rsk4 and Pdk1 genes during murine embryogenesis. Kohn, M., Hameister, H., Vogel, M., Kehrer-Sawatzki, H. Gene Expr. Patterns (2003) [Pubmed]
  13. Salicylic acid and aspirin inhibit the activity of RSK2 kinase and repress RSK2-dependent transcription of cyclic AMP response element binding protein- and NF-kappa B-responsive genes. Stevenson, M.A., Zhao, M.J., Asea, A., Coleman, C.N., Calderwood, S.K. J. Immunol. (1999) [Pubmed]
  14. 90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. Jensen, C.J., Buch, M.B., Krag, T.O., Hemmings, B.A., Gammeltoft, S., Frödin, M. J. Biol. Chem. (1999) [Pubmed]
  15. Ribosomal S6 kinase 2 interacts with and phosphorylates PDZ domain-containing proteins and regulates AMPA receptor transmission. Thomas, G.M., Rumbaugh, G.R., Harrar, D.B., Huganir, R.L. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  16. Ser-10 phosphorylation of histone H3 and immediate early gene expression in oncogene-transformed mouse fibroblasts. Strelkov, I.S., Davie, J.R. Cancer Res. (2002) [Pubmed]
  17. Macrophage inflammatory protein 2 inhibits beta-amyloid peptide (1-42)-mediated hippocampal neuronal apoptosis through activation of mitogen-activated protein kinase and phosphatidylinositol 3-kinase signaling pathways. Watson, K., Fan, G.H. Mol. Pharmacol. (2005) [Pubmed]
  18. The vaccinia virus-stimulated mitogen-activated protein kinase (MAPK) pathway is required for virus multiplication. Andrade, A.A., Silva, P.N., Pereira, A.C., De Sousa, L.P., Ferreira, P.C., Gazzinelli, R.T., Kroon, E.G., Ropert, C., Bonjardim, C.A. Biochem. J. (2004) [Pubmed]
  19. Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1. Zhong, S., Jansen, C., She, Q.B., Goto, H., Inagaki, M., Bode, A.M., Ma, W.Y., Dong, Z. J. Biol. Chem. (2001) [Pubmed]
  20. Coupling cAMP signaling to transcription in the liver: pivotal role of CREB and CREM. Servillo, G., Della Fazia, M.A., Sassone-Corsi, P. Exp. Cell Res. (2002) [Pubmed]
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