RPS6KA5
Ribosomal protein S6 kinase alpha-5 is an enzyme that in humans is encoded by the RPS6KA5 gene.[1][2][3]
Interactions
RPS6KA5 has been shown to interact with CREB1.[1][4]
References
- ↑ 1.0 1.1 Deak M, Clifton AD, Lucocq LM, Alessi DR (September 1998). “Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB”. EMBO J. 17 (15): 4426–41. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
- ↑ Jiang C, Yu L, Tu Q, Zhao Y, Zhang H, Zhao S (April 2000). “Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31→q32.1 by radiation hybrid mapping”. Cytogenet Cell Genet. 87 (3–4): 261–2. doi:10.1159/000015441. PMID 10702687.
- ↑ “Entrez Gene: RPS6KA5 ribosomal protein S6 kinase, 90kDa, polypeptide 5”.
- ↑ Wang, X; Li W; Williams M; Terada N; Alessi D R; Proud C G (August 2001). “Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase”. EMBO J. England. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. ISSN 0261-4189. PMC 125559. PMID 11500364.
Further reading
- Chung J, Uchida E, Grammer TC, Blenis J (1997). “STAT3 serine phosphorylation by ERK-dependent and -independent pathways negatively modulates its tyrosine phosphorylation”. Mol. Cell. Biol. 17 (11): 6508–16. PMC 232504. PMID 9343414.
- Jain N, Zhang T, Fong SL, et al. (1999). “Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK)”. Oncogene. 17 (24): 3157–67. doi:10.1038/sj.onc.1202238. PMID 9872331.
- New L, Zhao M, Li Y, et al. (1999). “Cloning and characterization of RLPK, a novel RSK-related protein kinase”. J. Biol. Chem. 274 (2): 1026–32. doi:10.1074/jbc.274.2.1026. PMID 9873047.
- Thomson S, Clayton AL, Hazzalin CA, et al. (1999). “The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase”. EMBO J. 18 (17): 4779–93. doi:10.1093/emboj/18.17.4779. PMC 1171550. PMID 10469656.
- Lim CP, Cao X (1999). “Serine phosphorylation and negative regulation of Stat3 by JNK”. J. Biol. Chem. 274 (43): 31055–61. doi:10.1074/jbc.274.43.31055. PMID 10521505.
- Buck M, Poli V, van der Geer P, et al. (2000). “Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha”. Mol. Cell. 4 (6): 1087–92. doi:10.1016/S1097-2765(00)80237-3. PMID 10635333.
- Lizcano JM, Morrice N, Cohen P (2001). “Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155”. Biochem. J. 349 (Pt 2): 547–57. doi:10.1042/0264-6021:3490547. PMC 1221178. PMID 10880354.
- Hefner Y, Borsch-Haubold AG, Murakami M, et al. (2001). “Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases”. J. Biol. Chem. 275 (48): 37542–51. doi:10.1074/jbc.M003395200. PMID 10978317.
- Arthur JS, Cohen P (2000). “MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells”. FEBS Lett. 482 (1–2): 44–8. doi:10.1016/S0014-5793(00)02031-7. PMID 11018520.
- Sapkota GP, Kieloch A, Lizcano JM, et al. (2001). “Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth”. J. Biol. Chem. 276 (22): 19469–82. doi:10.1074/jbc.M009953200. PMID 11297520.
- Deb A, Zamanian-Daryoush M, Xu Z, et al. (2001). “Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3”. EMBO J. 20 (10): 2487–96. doi:10.1093/emboj/20.10.2487. PMC 125453. PMID 11350938.
- Liu G, Zhang Y, Bode AM, et al. (2002). “Phosphorylation of 4E-BP1 is mediated by the p38/MSK1 pathway in response to UVB irradiation”. J. Biol. Chem. 277 (11): 8810–6. doi:10.1074/jbc.M110477200. PMID 11777913.
- Wiggin GR, Soloaga A, Foster JM, et al. (2002). “MSK1 and MSK2 Are Required for the Mitogen- and Stress-Induced Phosphorylation of CREB and ATF1 in Fibroblasts”. Mol. Cell. Biol. 22 (8): 2871–81. doi:10.1128/MCB.22.8.2871-2881.2002. PMC 133730. PMID 11909979.
- Markou T, Lazou A (2002). “Phosphorylation and activation of mitogen- and stress-activated protein kinase-1 in adult rat cardiac myocytes by G-protein-coupled receptor agonists requires both extracellular-signal-regulated kinase and p38 mitogen-activated protein kinase”. Biochem. J. 365 (Pt 3): 757–63. doi:10.1042/BJ20011828. PMC 1222733. PMID 11994045.
- Toska K, Kleppe R, Armstrong CG, et al. (2002). “Regulation of tyrosine hydroxylase by stress-activated protein kinases”. J. Neurochem. 83 (4): 775–83. doi:10.1046/j.1471-4159.2002.01172.x. PMID 12421349.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Janknecht R (2003). “Regulation of the ER81 transcription factor and its coactivators by mitogen- and stress-activated protein kinase 1 (MSK1)”. Oncogene. 22 (5): 746–55. doi:10.1038/sj.onc.1206185. PMID 12569367.
- Dolled-Filhart M, Camp RL, Kowalski DP, et al. (2003). “Tissue microarray analysis of signal transducers and activators of transcription 3 (Stat3) and phospho-Stat3 (Tyr705) in node-negative breast cancer shows nuclear localization is associated with a better prognosis”. Clin. Cancer Res. 9 (2): 594–600. PMID 12576423.
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