RPS6KA2
Ribosomal protein S6 kinase alpha-2 is an enzyme that in humans is encoded by the RPS6KA2 gene.[1][2]
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine and threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[2]
References
References
- ↑ Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M (Apr 1994). “Human rsk isoforms: cloning and characterization of tissue-specific expression”. Am J Physiol. 266 (2 Pt 1): C351–9. PMID 8141249.
- ↑ 2.0 2.1 “Entrez Gene: RPS6KA2 ribosomal protein S6 kinase, 90kDa, polypeptide 2”.
- ↑ 3.0 3.1 Roux, Philippe P; Richards Stephanie A; Blenis John (Jul 2003). “Phosphorylation of p90 Ribosomal S6 Kinase (RSK) Regulates Extracellular Signal-Regulated Kinase Docking and RSK Activity”. Mol. Cell. Biol. United States. 23 (14): 4796–804. doi:10.1128/MCB.23.14.4796-4804.2003. ISSN 0270-7306. PMC 162206. PMID 12832467.
- ↑ 4.0 4.1 Zhao, Y; Bjorbaek C; Moller D E (Nov 1996). “Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. UNITED STATES. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. ISSN 0021-9258. PMID 8939914.
Further reading
Further reading
- Dawson SJ, White LA (1992). “Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin”. J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Zhao Y, Bjørbaek C, Weremowicz S, et al. (1995). “RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation”. Mol. Cell. Biol. 15 (8): 4353–63. PMC 230675. PMID 7623830.
- Wong EV, Schaefer AW, Landreth G, Lemmon V (1996). “Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1”. J. Biol. Chem. 271 (30): 18217–23. doi:10.1074/jbc.271.30.18217. PMID 8663493.
- Xing J, Ginty DD, Greenberg ME (1996). “Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase”. Science. 273 (5277): 959–63. Bibcode:1996Sci…273..959X. doi:10.1126/science.273.5277.959. PMID 8688081.
- Zhao Y, Bjorbaek C, Moller DE (1997). “Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases”. J. Biol. Chem. 271 (47): 29773–9. doi:10.1074/jbc.271.47.29773. PMID 8939914.
- Fukunaga R, Hunter T (1997). “MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates”. EMBO J. 16 (8): 1921–33. doi:10.1093/emboj/16.8.1921. PMC 1169795. PMID 9155018.
- del Peso L, González-García M, Page C, et al. (1997). “Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt”. Science. 278 (5338): 687–9. doi:10.1126/science.278.5338.687. PMID 9381178.
- Deak M, Clifton AD, Lucocq LM, Alessi DR (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.
- Du K, Montminy M (1999). “CREB is a regulatory target for the protein kinase Akt/PKB”. J. Biol. Chem. 273 (49): 32377–9. doi:10.1074/jbc.273.49.32377. PMID 9829964.
- Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW (1999). “Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo”. J. Biol. Chem. 274 (5): 2893–8. doi:10.1074/jbc.274.5.2893. PMID 9915826.
- Jensen CJ, Buch MB, Krag TO, et al. (1999). “90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1”. J. Biol. Chem. 274 (38): 27168–76. doi:10.1074/jbc.274.38.27168. PMID 10480933.
- Schimenti JC (2000). “ORFless, intronless, and mutant transcription units in the mouse t complex responder (Tcr) locus”. Mamm. Genome. 10 (10): 969–76. doi:10.1007/s003359901142. PMID 10501965.
- Scheid MP, Schubert KM, Duronio V (1999). “Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase”. J. Biol. Chem. 274 (43): 31108–13. doi:10.1074/jbc.274.43.31108. PMID 10521512.
- Tan Y, Demeter MR, Ruan H, Comb MJ (2000). “BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival”. J. Biol. Chem. 275 (33): 25865–9. doi:10.1074/jbc.M004199200. PMID 10837486.
- 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.
- Datta SR, Katsov A, Hu L, et al. (2000). “14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation”. Mol. Cell. 6 (1): 41–51. doi:10.1016/S1097-2765(00)00006-X. PMID 10949026.
- Gudi T, Casteel DE, Vinson C, et al. (2001). “NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation”. Oncogene. 19 (54): 6324–33. doi:10.1038/sj.onc.1204007. PMID 11175347.
- Willard FS, Crouch MF (2001). “MEK, ERK, and p90RSK are present on mitotic tubulin in Swiss 3T3 cells: a role for the MAP kinase pathway in regulating mitotic exit”. Cell. Signal. 13 (9): 653–64. doi:10.1016/S0898-6568(01)00185-1. PMID 11495723.
- Schinelli S, Zanassi P, Paolillo M, et al. (2001). “Stimulation of endothelin B receptors in astrocytes induces cAMP response element-binding protein phosphorylation and c-fos expression via multiple mitogen-activated protein kinase signaling pathways”. J. Neurosci. 21 (22): 8842–53. PMID 11698596.
Looking for the patient version?
© 2026 MyEClinic – IFTM Institut für Telematik in der Medizin GmbH