RPS6KA1 (ribosomal protein S6 kinase, 90kDa, polypeptide 1)

Identity

Other names	HU-1
	MAPKAPK1A
	RSK
	RSK1
	p90S6K
	pp90RSK1
HGNC	RPS6KA1
Location	1p36.11
Local_order	Information about the local order of the human RPS6KA1 locus can be found at ensembl.org. Human RPS6KA1 is found on chromosome 1, position 26,744,930-26,774,107, between genes coding for HMGN2 (High-mobility group nucleosome-binding domain-containing protein 2) and ARID1A (AT-rich interactive domain-containing protein 1A).

Note	The commonly used named for RPS6KA1 is RSK1, which will be used hereafter.

DNA/RNA

Note	RSK1 was the first cloned isoform of the p90 ribosomal S6 kinase family, which now contains three other members (RSK2, RSK3 and RSK4).
Description	The genomic size of the entire RSK1 gene is about 45,260 bp and is located on the + strand of chromosome 1. This gene contains 22 coding exons.
Transcription	The length of the transcript is 3,186 bp, from which the open reading frame contains 2,208 bp. While the 5'UTR contains 154 bp, the 3'UTR contains 824 bp.
Pseudogene	No human pseudogene known.

Protein

	The RSK1 protein contains two kinase domains separated by a linker region of about 100 aa. While the N-terminal kinase domain (NTKD) belongs to the AGC family of kinases, the C-terminal kinase domain (CTKD) belongs to the CaMK family. RSK1 activation requires its interaction with ERK1 and ERK2 through its C-terminal ERK docking region, which initiates an ordered phosphorylation sequence leading to the phosphorylation of six serine or threonine residues (S221, T359, S363, S380, T573 and S732).

Description	The RSK1 protein consists of 735 amino acids, with an apparent molecular weight of about 85-90 kDa.
Expression	Northern analyses and RNase protection assays revealed that RSK1 is expressed in many tissues, with higher levels in skeletal muscle, kidney, lung, liver, pancreas, spleen, thymus, and brain. Although other RSK isoforms are expressed ubiquitously in the brain, RSK1 is most abundant in the cerebellum. In situ hybridization of mouse embryonic tissues revealed that RSK1 is strongly expressed in regions harbouring highly proliferating cells. These include liver, lung, and thymus, as well as olfactory, respiratory, and gut epithelia.
Localisation	RSK1 is normally present in the cytoplasm, but upon mitogenic stimulation it moves into the nucleus, where it phosphorylates several substrates involved in gene transcription. Within minutes of stimulation, RSK1 was shown to accumulate transiently at the plasma membrane, where it presumably receives additional inputs necessary for activation before nuclear translocation.
Function	Mitogenic stimulation of the Ras/ERK pathway leads to the activation of RSK1. RSK1 seems to be a multifunctional ERK effector because it participates in various cellular processes, including nuclear signalling. RSK1 was found to regulate several transcription factors, including SRF, c-Fos, and Nur77. Additional nuclear factors have been shown to be regulated by RSK1, including MITF, estrogen receptor-a nuclear factor (NF)-ATc4 and ER81. RSK1 was shown to interact with the transcriptional coactivator CREB-binding protein (CBP), which, interestingly, binds many transcription factors known to be regulated by RSK1. On the basis of the nature of its substrates, RSK1 seems to have important functions in cellular growth control and proliferation. RSK1 may stimulate cell cycle progression through the regulation of immediate early gene products, such as c-Fos, which promotes the expression of cyclin D1 during the G0/G1 transition to S phase. Other proteins through which RSK1 may stimulate proliferation include the cyclin-dependent kinase (CDK) inhibitor p27kip1, the Na+/H+ exchanger NHE-1 and the kinase GSK3. RSK1 has been shown to phosphorylate and inhibit neuronal NO synthase in response to mitogenic signaling. RSK1 may also promote proliferation by regulating cell-growth-related protein synthesis. Indeed, RSK1 was shown to phosphorylate the tumour suppressor proteins TSC2 and LKB1, thereby resulting in increased mTOR signalling and mRNA translation.
Homology	The RSK family contains four human isoforms (RSK1, RSK2, RSK3 and RSK4), which share 65-73% aa identity. RSK-related molecules have also been identified in C. elegans (T01H8.1) and D. melanogaster (RPS6-protein kinase-II), which share around 50% aa identity to human RSK1 and also contain the two kinase domains typical to RSK family members. No RSK homologues have been found in yeast or plant.

Mutations

Somatic

The natural variant K335T has been observed.

Implicated in

Entity	Various cancers
Prognosis	Frequent activation of the Ras/ERK signalling pathway has been reported in a broad range of human cancers including various carcinomas, glioblastomas and hematological malignancies. In some of these tumour types, RSK1 expression has been shown to be increased, such as in cancers of the breast and prostate.
	Hyperactivation of RSK has been reported in multiple cancers. Activation of growth factor receptors either by ligand stimulation or receptor overexpression/mutation are common mechanisms that lead to RSK activation. RSK is now known to be a central player in a signalling pathway consisting of many components that have been implicated in tumorigenesis, including upstream Ras GTPases and Raf kinases.
Oncogenesis	RSK1 is an important mediator of survival signals that protect cells from undergoing apoptosis and, thus, is a potentially important therapeutic target. Inhibition of RSK activity using the pharmacological inhibitor SL-0101 was shown to reduce the proliferation rates of breast cancer cells, but not normal breast epithelial cells.

External links

	Nomenclature
HGNC	RPS6KA1   10430
Entrez_Gene	RPS6KA1  6195  ribosomal protein S6 kinase, 90kDa, polypeptide 1
	Cards
GeneCards	RPS6KA1
Ensembl	RPS6KA1 [Search_View]   ENSG00000117676 [Gene_View]
Genatlas	RPS6KA1
GeneLynx	RPS6KA1
eGenome	RPS6KA1
euGene	6195
	Genomic and cartography
GoldenPath	RPS6KA1  -  1p36.11   chr1:26744930-26774107 +  1p   [Description]    (hg18-Mar_2006)
Ensembl	RPS6KA1 - 1p [CytoView]
NCBI	Mapview
OMIM	Disease map [OMIM]
HomoloGene	RPS6KA1
	Gene and transcription
Genbank	AK092955 [ ENTREZ ]
Genbank	AK225672 [ ENTREZ ]
Genbank	AK292722 [ ENTREZ ]
Genbank	AK315730 [ ENTREZ ]
Genbank	BC014966 [ ENTREZ ]
RefSeq	NM_001006665 [ SRS ]    NM_001006665 [ ENTREZ ]
RefSeq	NM_002953 [ SRS ]    NM_002953 [ ENTREZ ]
RefSeq	AC_000044 [ SRS ]    AC_000044 [ ENTREZ ]
RefSeq	AC_000133 [ SRS ]    AC_000133 [ ENTREZ ]
RefSeq	NC_000001 [ SRS ]    NC_000001 [ ENTREZ ]
RefSeq	NT_004610 [ SRS ]    NT_004610 [ ENTREZ ]
RefSeq	NW_001838576 [ SRS ]    NW_001838576 [ ENTREZ ]
RefSeq	NW_921351 [ SRS ]    NW_921351 [ ENTREZ ]
AceView	RPS6KA1 AceView - NCBI
Unigene	Hs.149957 [ SRS ]    Hs.149957 [ NCBI ]     HS149957 [ spliceNest ]
Fast-db	11122 (alternative variants)
	Protein : pattern, domain, 3D structure
SwissProt	Q15418 [ SRS]    Q15418 [ EXPASY ]     Q15418 [ INTERPRO ]     Q15418 [ UNIPROT ]
Prosite	PS51285 AGC_KINASE_CTER [ SRS ]    PS51285 AGC_KINASE_CTER [ Expasy ]
Prosite	PS00107 PROTEIN_KINASE_ATP [ SRS ]    PS00107 PROTEIN_KINASE_ATP [ Expasy ]
Prosite	PS50011 PROTEIN_KINASE_DOM [ SRS ]    PS50011 PROTEIN_KINASE_DOM [ Expasy ]
Prosite	PS00108 PROTEIN_KINASE_ST [ SRS ]    PS00108 PROTEIN_KINASE_ST [ Expasy ]
Interpro	IPR000961 Pkinase_C [ SRS ]    IPR000961 Pkinase_C [ EBI ]
Interpro	IPR000719 Prot_kinase_core [ SRS ]    IPR000719 Prot_kinase_core [ EBI ]
Interpro	IPR017441 Protein_kinase_ATP_bd_CS [ SRS ]    IPR017441 Protein_kinase_ATP_bd_CS [ EBI ]
Interpro	IPR016239 Ribosomal_S6_kinase_II [ SRS ]    IPR016239 Ribosomal_S6_kinase_II [ EBI ]
Interpro	IPR017442 Se/Thr_pkinase-rel [ SRS ]    IPR017442 Se/Thr_pkinase-rel [ EBI ]
Interpro	IPR008271 Ser_thr_pkin_AS [ SRS ]    IPR008271 Ser_thr_pkin_AS [ EBI ]
Interpro	IPR002290 Ser_thr_pkinase [ SRS ]    IPR002290 Ser_thr_pkinase [ EBI ]
CluSTr	Q15418
Pfam	PF00069 Pkinase [ SRS ]    PF00069 Pkinase [ Sanger ]    pfam00069 [ NCBI-CDD ]
Pfam	PF00433 Pkinase_C [ SRS ]    PF00433 Pkinase_C [ Sanger ]    pfam00433 [ NCBI-CDD ]
Smart	SM00133 S_TK_X [EMBL]
Smart	SM00220 S_TKc [EMBL]
Prodom	PD000001 Prot_kinase[INRA-Toulouse]
Prodom	Q15418 KS6A1_HUMAN [ Domain structure ]   Q15418 KS6A1_HUMAN  [ sequences sharing at least 1 domain ]
Blocks	Q15418
PDB	2Z7Q [ SRS ]    2Z7Q [ PdbSum ],   2Z7Q [ IMB ]   2Z7Q [ RSDB ]
PDB	2Z7R [ SRS ]    2Z7R [ PdbSum ],   2Z7R [ IMB ]   2Z7R [ RSDB ]
PDB	2Z7S [ SRS ]    2Z7S [ PdbSum ],   2Z7S [ IMB ]   2Z7S [ RSDB ]
HPRD	03402
	Protein Interaction databases
DIP	Q15418
IntAct	Q15418
	Polymorphism : SNP, mutations, diseases
OMIM	601684    [ map ]
GENECLINICS	601684
SNP	RPS6KA1 [dbSNP-NCBI]
SNP	NM_001006665 [SNP-NCI]
SNP	NM_002953 [SNP-NCI]
SNP	RPS6KA1 [GeneSNPs - Utah]  RPS6KA1] [HGBASE - SRS]
HAPMAP	RPS6KA1 [HAPMAP]
COSMIC	RPS6KA1 [Somatic mutation (COSMIC-CGP-Sanger)]
HGMD	RPS6KA1
	General knowledge
Family Browser	RPS6KA1 [UCSC Family Browser]
SOURCE	NM_001006665
SOURCE	NM_002953
SMD	Hs.149957
SAGE	Hs.149957
Enzyme	2.7.11.1 [ Enzyme-Expasy ]   2.7.11.1 [ Enzyme-SRS ]   2.7.11.1 [ IntEnz-EBI ]   2.7.11.1 [ BRENDA ]   2.7.11.1 [ KEGG ]   2.7.11.1 [ WIT ]
GO	nucleotide binding [Amigo]  nucleotide binding
GO	magnesium ion binding [Amigo]  magnesium ion binding
GO	protein serine/threonine kinase activity [Amigo]  protein serine/threonine kinase activity
GO	protein serine/threonine kinase activity [Amigo]  protein serine/threonine kinase activity
GO	protein binding [Amigo]  protein binding
GO	ATP binding [Amigo]  ATP binding
GO	nucleoplasm [Amigo]  nucleoplasm
GO	protein amino acid phosphorylation [Amigo]  protein amino acid phosphorylation
GO	signal transduction [Amigo]  signal transduction
GO	protein kinase cascade [Amigo]  protein kinase cascade
GO	transferase activity [Amigo]  transferase activity
BIOCARTA	Regulation of BAD phosphorylation    [Genes]
BIOCARTA	Transcription factor CREB and its extracellular signals    [Genes]
BIOCARTA	Role of Erk5 in Neuronal Survival    [Genes]
BIOCARTA	Erk1/Erk2 Mapk Signaling pathway    [Genes]
BIOCARTA	Cell Cycle: G2/M Checkpoint    [Genes]
BIOCARTA	Growth Hormone Signaling Pathway    [Genes]
BIOCARTA	Multiple antiapoptotic pathways from IGF-1R signaling lead to BAD phosphorylation    [Genes]
BIOCARTA	How Progesterone Initiates the Oocyte Maturation    [Genes]
BIOCARTA	MAPKinase Signaling Pathway    [Genes]
BIOCARTA	Melanocyte Development and Pigmentation    [Genes]
KEGG	MAPK signaling pathway
KEGG	mTOR signaling pathway
KEGG	Long-term potentiation
PubGene	RPS6KA1
TreeFam	RPS6KA1
CTD	6195 [Comparative ToxicoGenomics Database]
	Other databases
	Probes
Probe	RPS6KA1 Related clones (RZPD - Berlin)
	PubMed
PubMed	93 Pubmed reference(s) in LocusLink

Bibliography

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PMID 3856226

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PMID 2779569

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PMID 1648378

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PMID 1545823

Cytoplasmic to nuclear signal transduction by mitogen-activated protein kinase and 90 kDa ribosomal S6 kinase.

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PMID 8132089

Functional domains and phosphorylation of the orphan receptor Nur77.

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Molecular Endocrinology 1993; 7: 953-964.

PMID 8232315

Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2.

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PMID 7901013

Human rsk isoforms: cloning and characterization of tissue-specific expression.

Moller DE, Xia CH, Tang W, Zhu AX, Jakubowski M.

American Journal of Physiology 1994; 266: 351-359.

PMID 8141249

Evidence that inactive p42 mitogen-activated protein kinase and inactive Rsk exist as a heterodimer in vivo.

Hsiao K-M, Chou S-Y, Shih S-J, Ferrell JE Jr.

Proc Natl Acad Sci USA 1994; 91: 5480-5484.

PMID 8202512

The signal-dependent coactivator CBP is a nuclear target for pp90RSK.

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Cell 1996; 86: 465-474.

PMID 8756728

Evidence for two catalytically active kinase domains in pp90rsk.

Fisher TL, Blenis J.

Mol Cell Biol 1996; 16: 1212-1219.

PMID 8622665

Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases.

Zhao Y, Bjorbaek C, Moller DE.

J Biol Chem 1996; 271: 29773-29779.

PMID 8939914

The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IkappaBalpha and stimulates its degradation in vitro.

Ghoda L, Lin X, Greene WC.

J Biol Chem 1997; 272: 21281-21288.

PMID 9261139

Identification of serine 380 as the major site of autophosphorylation of Xenopus pp90rsk.

Vik TA, Ryder JW.

Biochem Biophys Res Commun 1997; 235: 398-402.

PMID 9199205

IκBα is a target for the mitogen-activated 90 kDa ribosomal S6 kinase.

Schouten GJ, Vertegaal ACO, Whiteside ST, Israel A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A.

EMBO J 1997; 16: 3133-3144.

PMID 9214631

A link between MAP kinase and p34(cdc2)/cyclin B during oocyte maturation: p90(rsk) phosphorylates and inactivates the p34(cdc2) inhibitory kinase Myt1.

Palmer A, Gavin AC, Nebreda AR.

Embo J 1998; 17: 5037-5047.

PMID 9724639

Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK.

Dalby KN, Morrice N, Caudwell FB, Avruch J, Cohen P.

J Biol Chem 1998; 273: 1496-1505.

PMID 9430688

pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167.

Joel PB, Smith J, Sturgill TW, Fisher TL, Blenis J, Lannigan DA.

Mol Cell Biol 1998; 18: 1978-1984.

PMID 9528769

A p90(rsk) mutant constitutively interacting with MAP kinase uncouples MAP kinase from p34(cdc2)/cyclin B activation in Xenopus oocytes.

Gavin AC, Ni Ainle A, Chierici E, Jones M, Nebreda AR.

Mol Biol Cell 1999; 10: 2971-2986.

PMID 10473640

90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1.

Jensen CJ, Buch MB, Krag TO, Hemmings BA, Gammeltoft S, Frodin M.

J Biol Chem 1999; 274: 27168-27176.

PMID 10480933

Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK.

Richards SA, Fu J, Romanelli A, Shimamura A, Blenis J.

Curr Biol 1999; 9: 810-820.

PMID 10469565

Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo.

Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW.

J Biol Chem 1999; 274: 2893-2898.

PMID 9915826

p90(RSK) is a serum-stimulated Na+/H+ exchanger isoform-1 kinase. Regulatory phosphorylation of serine 703 of Na+/H+ exchanger isoform-1.

Takahashi E, Abe J, Gallis B, Aebersold R, Spring DJ, Krebs EG, Berk BC.

J Biol Chem 1999; 274: 20206-20214.

PMID 10400637

A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.

Frodin M, Jensen CJ, Merienne K, Gammeltoft S.

Embo J 2000; 19: 2924-2934.

PMID 10856237

Rsk1 mediates a MEK-MAP kinase cell survival signal.

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Curr Biol 2000; 10: 127-135.

PMID 10679322

Characterization of regulatory events associated with membrane targeting of p90 ribosomal S6 kinase 1.

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Mol Cell Biol 2001; 21: 7470-7480.

PMID 11585927

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.

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J Biol Chem 2001; 276: 19469-19482.

PMID 11297520

Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase.

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Embo J 2001; 20: 4370-4379.

PMID 11500364

Bub1 is activated by the protein kinase p90(Rsk) during Xenopus oocyte maturation.

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Curr Biol 2001; 11: 141-150.

PMID 11231148

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PMID 12374740

Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity.

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Mol Cell Biol 2003; 23: 4796-4804.

PMID 12832467

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J Biol Chem 2003; 278: 49254-49260.

PMID 14504289

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PMID 15525759

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PMID 15342917

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PMID 15187187

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The Tumor Suppressor DAP Kinase Is a Target of RSK-Mediated Survival Signaling.

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Curr Biol 2005; 15: 1762-1767.

PMID 16213824

Structural bioinformatics-based design of selective, irreversible kinase inhibitors.

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PMID 15919995

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J Cell Biol 2005; 169: 227-231.

PMID 15837801

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PMID 15893597

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PMID 15539959

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Mol Cell Biol 2005; 25: 907-920.

PMID 15657420

Subcellular localization and biological actions of activated RSK1 are determined by its interactions with subunits of cyclic AMP-dependent protein kinase.

Chaturvedi D, Poppleton HM, Stringfield T, Barbier A, Patel TB.

Mol Cell Biol 2006; 26: 4586-4600.

PMID 16738324

The MAP kinase ERK5 binds to and phosphorylates p90 RSK.

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Arch Biochem Biophys 2006; 449: 8-16.

PMID 16626623

Hauge C, Frodin M.

J Cell Sci 2006; 119: 3021-3023.

PMID 16868029

The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity.

Shahbazian D, Roux PP, Mieulet V, Cohen MS, Raught B, Taunton J, Hershey JW, Blenis J, Pende M, Sonenberg N.

Embo J 2006; 25: 2781-2791.

PMID 16763566

Inhibition of ERK-MAP kinase signaling by RSK during Drosophila development.

Kim M, Lee JH, Koh H, Lee SY, Jang C, Chung CJ, Sung JH, Blenis J, Chung J.

Embo J 2006; 25: 3056-3067.

PMID 16763554

Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation.

Wingate AD, Campbell DG, Peggie M, Arthur JS.

Biochem J 2006; 393: 715-724.

PMID 16223362

A clickable inhibitor reveals context-dependent autoactivation of p90 RSK.

Cohen MS, Hadjivassiliou H, Taunton J.

Nat Chem Biol 2007; 3: 156-160.

PMID 17259979

RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation.

Roux PP, Shahbazian D, Vu H, Holz MK, Cohen MS, Taunton J, Sonenberg N, Blenis J.

J Biol Chem 2007; 282: 14056-14064.

PMID 17360704

BI-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo.

Sapkota GP, Cummings L, Newell FS, Armstrong C, Bain J, Frodin M, Grauert M, Hoffmann M, Schnapp G, Steegmaier M, Cohen P, Alessi DR.

Biochem J 2007; 401: 29-38.

PMID 17040210

p90 RSK-1 associates with and inhibits neuronal nitric oxide synthase.

Song T, Sugimoto K, Ihara H, Mizutani A, Hatano N, Kume K, Kambe T, Yamaguchi F, Tokuda M, Watanabe Y.

Biochem J 2007; 401: 391-398.

PMID 16984226

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Contributor(s)

Written	03-2008	Philippe P Roux
		Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, P.O. Box 6128, Station Centre-Ville, Montreal QC H3C 3J7, Canada

Citation

This paper should be referenced as such :

© Atlas of Genetics and Cytogenetics in Oncology and Haematology

indexed on : Mon Aug 11 21:17:17 2008