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Ribosomal protein S6 kinase beta-2 is an enzyme that in humans is encoded by the RPS6KB2gene.[1][2][3]
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains two nonidentical kinase catalytic domains and phosphorilates the S6 ribosomal protein and eucaryotic translation initiation factor 4B (eIF4B). Phosphorylation of S6 leads to an increase in protein synthesis and cell proliferation.[3]
References
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↑Gout I, Minami T, Hara K, Tsujishita Y, Filonenko V, Waterfield MD, Yonezawa K (Dec 1998). "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region". J Biol Chem. 273 (46): 30061–30064. doi:10.1074/jbc.273.46.30061. PMID9804755.
Lee-Fruman KK, Kuo CJ, Lippincott J, et al. (1999). "Characterization of S6K2, a novel kinase homologous to S6K1". Oncogene. 18 (36): 5108–5114. doi:10.1038/sj.onc.1202894. PMID10490847.
Koh H, Jee K, Lee B, et al. (1999). "Cloning and characterization of a nuclear S6 kinase, S6 kinase-related kinase (SRK); a novel nuclear target of Akt". Oncogene. 18 (36): 5115–5119. doi:10.1038/sj.onc.1202895. PMID10490848.
Martin KA, Schalm SS, Richardson C, et al. (2001). "Regulation of ribosomal S6 kinase 2 by effectors of the phosphoinositide 3-kinase pathway". J. Biol. Chem. 276 (11): 7884–7891. doi:10.1074/jbc.M006969200. PMID11108711.
Martin KA, Schalm SS, Romanelli A, et al. (2001). "Ribosomal S6 kinase 2 inhibition by a potent C-terminal repressor domain is relieved by mitogen-activated protein-extracellular signal-regulated kinase kinase-regulated phosphorylation". J. Biol. Chem. 276 (11): 7892–7898. doi:10.1074/jbc.M009972200. PMID11108720.
Minami T, Hara K, Oshiro N, et al. (2002). "Distinct regulatory mechanism for p70 S6 kinase beta from that for p70 S6 kinase alpha". Genes Cells. 6 (11): 1003–1015. doi:10.1046/j.1365-2443.2001.00479.x. PMID11733037.
Pardo OE, Arcaro A, Salerno G, et al. (2002). "Novel cross talk between MEK and S6K2 in FGF-2 induced proliferation of SCLC cells". Oncogene. 20 (52): 7658–7667. doi:10.1038/sj.onc.1204994. PMID11753643.
Park IH, Bachmann R, Shirazi H, Chen J (2002). "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin". J. Biol. Chem. 277 (35): 31423–31429. doi:10.1074/jbc.M204080200. PMID12087098.
Kanayasu-Toyoda T, Yamaguchi T, Oshizawa T, et al. (2002). "Role of the p70 S6 kinase cascade in neutrophilic differentiation and proliferation of HL-60 cells-a study of transferrin receptor-positive and -negative cells obtained from dimethyl sulfoxide- or retinoic acid-treated HL-60 cells". Arch. Biochem. Biophys. 405 (1): 21–31. doi:10.1016/S0003-9861(02)00330-2. PMID12176053.
Levy Y, Ronen D, Bershadsky AD, Zick Y (2003). "Sustained induction of ERK, protein kinase B, and p70 S6 kinase regulates cell spreading and formation of F-actin microspikes upon ligation of integrins by galectin-8, a mammalian lectin". J. Biol. Chem. 278 (16): 14533–14542. doi:10.1074/jbc.M207380200. PMID12569102.
Kanayasu-Toyoda T, Yamaguchi T, Oshizawa T, et al. (2003). "The role of c-Myc on granulocyte colony-stimulating factor-dependent neutrophilic proliferation and differentiation of HL-60 cells". Biochem. Pharmacol. 66 (1): 133–140. doi:10.1016/S0006-2952(03)00247-8. PMID12818373.
Shao J, Evers BM, Sheng H (2004). "Roles of phosphatidylinositol 3'-kinase and mammalian target of rapamycin/p70 ribosomal protein S6 kinase in K-Ras-mediated transformation of intestinal epithelial cells". Cancer Res. 64 (1): 229–235. doi:10.1158/0008-5472.CAN-03-1859. PMID14729629.
Lekmine F, Sassano A, Uddin S, et al. (2004). "Interferon-gamma engages the p70 S6 kinase to regulate phosphorylation of the 40S S6 ribosomal protein". Exp. Cell Res. 295 (1): 173–182. doi:10.1016/j.yexcr.2003.12.021. PMID15051500.