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Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.[1] This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 nonidentical 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] [edit] Interactions RPS6KA1 has been shown to interact with YWHAB,[3] MAPK1,[4][5][6] IκBα,[7] TOB1[8] and TSC2.[9][10] [edit] See also [edit] 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.
- ^ "Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6195.
- ^ Cavet, Megan E; Lehoux Stephanie, Berk Bradford C (May. 2003). "14-3-3beta is a p90 ribosomal S6 kinase (RSK) isoform 1-binding protein that negatively regulates RSK kinase activity". J. Biol. Chem. (United States) 278 (20): 18376-83. doi:10.1074/jbc.M208475200. ISSN 0021-9258. PMID 12618428.
- ^ 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. ISSN 0270-7306. PMID 12832467.
- ^ Eblen, Scott T; Kumar N Vinay, Shah Kavita, Henderson Michelle J, Watts Colin K W, Shokat Kevan M, Weber Michael J (Apr. 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. (United States) 278 (17): 14926-35. doi:10.1074/jbc.M300485200. ISSN 0021-9258. PMID 12594221.
- ^ Smith, J A; Poteet-Smith C E, Malarkey K, Sturgill T W (Jan. 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. (UNITED STATES) 274 (5): 2893-8. ISSN 0021-9258. PMID 9915826.
- ^ Schouten, G J; Vertegaal A C, Whiteside S T, Israël A, Toebes M, Dorsman J C, van der Eb A J, Zantema A (Jun. 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. (ENGLAND) 16 (11): 3133-44. doi:10.1093/emboj/16.11.3133. ISSN 0261-4189. PMID 9214631.
- ^ Suzuki, T; Matsuda S, Tsuzuku J K, Yoshida Y, Yamamoto T (Feb. 2001). "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob". Genes Cells (England) 6 (2): 131-8. ISSN 1356-9597. PMID 11260258.
- ^ Roux, Philippe P; Ballif Bryan A, Anjum Rana, Gygi Steven P, Blenis John (Sep. 2004). "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (37): 13489-94. doi:10.1073/pnas.0405659101. ISSN 0027-8424. PMID 15342917.
- ^ Rolfe, Mark; McLeod Laura E, Pratt Phillip F, Proud Christopher G (Jun. 2005). "Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2)". Biochem. J. (England) 388 (Pt 3): 973-84. doi:10.1042/BJ20041888. PMID 15757502.
[edit] Further reading - Chen RH, Sarnecki C, Blenis J (1992). "Nuclear localization and regulation of erk- and rsk-encoded protein kinases.". Mol. Cell. Biol. 12 (3): 915–27. PMID 1545823.
- Tratner I, Ofir R, Verma IM (1992). "Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential.". Mol. Cell. Biol. 12 (3): 998–1006. PMID 1545828.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Chen RH, Abate C, Blenis J (1994). "Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase.". Proc. Natl. Acad. Sci. U.S.A. 90 (23): 10952–6. doi:10.1073/pnas.90.23.10952. PMID 8248197.
- Rivera VM, Miranti CK, Misra RP, et al. (1993). "A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.". Mol. Cell. Biol. 13 (10): 6260–73. PMID 8413226.
- Chen ZJ, Parent L, Maniatis T (1996). "Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity.". Cell 84 (6): 853–62. doi:10.1016/S0092-8674(00)81064-8. PMID 8601309.
- Barge RM, de Koning JP, Pouwels K, et al. (1996). "Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G-CSF-mediated activation of signaling complexes of the p21ras route.". Blood 87 (6): 2148–53. PMID 8630373.
- 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. doi:10.1126/science.273.5277.959. PMID 8688081.
- Nakajima T, Fukamizu A, Takahashi J, et al. (1996). "The signal-dependent coactivator CBP is a nuclear target for pp90RSK.". Cell 86 (3): 465–74. doi:10.1016/S0092-8674(00)80119-1. PMID 8756728.
- 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.
- Zaheer A, Lim R (1997). "Protein kinase A (PKA)- and protein kinase C-phosphorylated glia maturation factor promotes the catalytic activity of PKA.". J. Biol. Chem. 272 (8): 5183–6. doi:10.1074/jbc.272.8.5183. PMID 9030586.
- Schouten GJ, Vertegaal AC, Whiteside ST, et al. (1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase.". Embo J. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMID 9214631.
- Li HL, Forman MS, Kurosaki T, Puré E (1997). "Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cells.". J. Biol. Chem. 272 (29): 18200–8. doi:10.1074/jbc.272.29.18200. PMID 9218456.
- Chang YW, Traugh JA (1997). "Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation.". J. Biol. Chem. 272 (45): 28252–7. doi:10.1074/jbc.272.45.28252. PMID 9353277.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- 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.
- Dalby KN, Morrice N, Caudwell FB, et al. (1998). "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.". J. Biol. Chem. 273 (3): 1496–505. doi:10.1074/jbc.273.3.1496. PMID 9430688.
- Joel PB, Smith J, Sturgill TW, et al. (1998). "pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167.". Mol. Cell. Biol. 18 (4): 1978–84. PMID 9528769.
| Kinases: Serine/threonine-specific protein kinases | | | Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20) | | | | LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Protein kinase B ( AKT1, AKT2, AKT3), Ataxia telangiectasia mutated, Mammalian target of rapamycin, EIF-2 kinases ( PKR, HRI), Wee1 ( WEE1) | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | | - | | | | | | | | | | | | | | | | Protein kinase C, Protein kinase Cζ, PKC alpha, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Protein kinase N1, PKN2, PKN3, | | | | | | | | | | | | | | | | BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1 | | | | | | | | | | | | | | | | | Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30) | | | | | | | | CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1 | | | | | | | | Extracellular signal-regulated ( MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal ( MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein ( MAPK11, MAPK13, MAPK14) | | | | MAP kinase kinase kinases ( MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs ( ARAF, BRAF, KSR1, KSR2) MLKs ( MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK) CDC7 | | | | | | | | - | | | | - | | | | - | | | | Bone morphogenetic protein receptors ( BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Müllerian hormone receptor | | | | | | | |