RPS6KA4: Difference between revisions
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'''Ribosomal protein S6 kinase alpha-4''' is an [[enzyme]] that in humans is encoded by the ''RPS6KA4'' [[gene]].<ref name="pmid9792677">{{cite journal |vauthors=Pierrat B, Correia JS, Mary JL, Tomas-Zuber M, Lesslauer W | title = RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK) | journal = J Biol Chem | volume = 273 | issue = 45 | pages = 29661–29671 |date=Dec 1998 | pmid = 9792677 | pmc = | doi =10.1074/jbc.273.45.29661 }}</ref><ref name="pmid9687510">{{cite journal |vauthors=Deak M, Clifton AD, Lucocq LM, Alessi DR | title = Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB | journal = EMBO J | volume = 17 | issue = 15 | pages = 4426–4441 |date=Sep 1998 | pmid = 9687510 | pmc = 1170775 | doi = 10.1093/emboj/17.15.4426 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA4 ribosomal protein S6 kinase, 90kDa, polypeptide 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8986| accessdate = }}</ref> | |||
== Function == | |||
This gene encodes a member of the RSK ([[ribosomal S6 kinase]]) family of [[serine/threonine kinase]]s. This kinase contains 2 non-identical kinase catalytic domains and [[phosphorylates]] various substrates, including [[CREB1]] and [[c-Fos]]. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref name="entrez"/> | |||
== Interactions == | |||
RPS6KA4 has been shown to [[Protein-protein interaction|interact]] with [[MAPK14]].<ref name="pmid9792677"/> | |||
== References == | |||
{{reflist}} | |||
== Further reading == | |||
{{refbegin | 2}} | |||
{{PBB_Further_reading | |||
| citations = | |||
*{{cite journal |vauthors=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase |journal=Science |volume=273 |issue= 5277 |pages= 959–963 |year= 1996 |pmid= 8688081 |doi=10.1126/science.273.5277.959 }} | |||
*{{cite journal |vauthors=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377–32379 |year= 1999 |pmid= 9829964 |doi=10.1074/jbc.273.49.32377 }} | |||
*{{cite journal |vauthors=Tomás-Zuber M, Mary JL, Lesslauer W |title=Control sites of ribosomal S6 kinase B and persistent activation through tumor necrosis factor |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 23549–23558 |year= 2000 |pmid= 10806207 |doi= 10.1074/jbc.M002586200 }} | |||
*{{cite journal | author=Tomás-Zuber M |title=C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB) |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5892–5899 |year= 2001 |pmid= 11035004 |doi= 10.1074/jbc.M005822200 |name-list-format=vanc| author2=Mary JL | author3=Lamour F | display-authors=3 | last4=Bur | first4=D | last5=Lesslauer | first5=W }} | |||
*{{cite journal | author=Gudi T |title=NO activation of fos promoter elements requires nuclear translocation of G-kinase I and CREB phosphorylation but is independent of MAP kinase activation |journal=Oncogene |volume=19 |issue= 54 |pages= 6324–6333 |year= 2001 |pmid= 11175347 |doi= 10.1038/sj.onc.1204007 |name-list-format=vanc| author2=Casteel DE | author3=Vinson C | display-authors=3 | last4=Boss | first4=Gerry R | last5=Pilz | first5=Renate B }} | |||
*{{cite journal | author=Prymakowska-Bosak M |title=Mitotic phosphorylation prevents the binding of HMGN proteins to chromatin |journal=Mol. Cell. Biol. |volume=21 |issue= 15 |pages= 5169–5178 |year= 2001 |pmid= 11438671 |doi= 10.1128/MCB.21.15.5169-5178.2001 | pmc=87241 |name-list-format=vanc| author2=Misteli T | author3=Herrera JE | display-authors=3 | last4=Shirakawa | first4=H. | last5=Birger | first5=Y. | last6=Garfield | first6=S. | last7=Bustin | first7=M. }} | |||
*{{cite journal | author=Wiggin GR |title=MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts |journal=Mol. Cell. Biol. |volume=22 |issue= 8 |pages= 2871–2881 |year= 2002 |pmid= 11909979 |doi=10.1128/MCB.22.8.2871-2881.2002 | pmc=133730 |name-list-format=vanc| author2=Soloaga A | author3=Foster JM | display-authors=3 | last4=Murray-Tait | first4=V. | last5=Cohen | first5=P. | last6=Arthur | first6=J. S. C. }} | |||
*{{cite journal | author=Soloaga A |title=MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14 |journal=EMBO J. |volume=22 |issue= 11 |pages= 2788–2797 |year= 2003 |pmid= 12773393 |doi= 10.1093/emboj/cdg273 | pmc=156769 |name-list-format=vanc| author2=Thomson S | author3=Wiggin GR | display-authors=3 | last4=Rampersaud | first4=N | last5=Dyson | first5=MH | last6=Hazzalin | first6=CA | last7=Mahadevan | first7=LC | last8=Arthur | first8=JS }} | |||
*{{cite journal | author=Wissing J |title=Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry |journal=Mol. Cell. Proteomics |volume=6 |issue= 3 |pages= 537–547 |year= 2007 |pmid= 17192257 |doi= 10.1074/mcp.T600062-MCP200 |name-list-format=vanc| author2=Jänsch L | author3=Nimtz M | display-authors=3 | last4=Dieterich | first4=G. | last5=Hornberger | first5=R. | last6=Keri | first6=G. | last7=Wehland | first7=J. | last8=Daub | first8=H. }} | |||
*{{cite journal | author=Gesser B |title=Dimethylfumarate specifically inhibits the mitogen and stress-activated kinases 1 and 2 (MSK1/2): possible role for its anti-psoriatic effect |journal=J. Invest. Dermatol. |volume=127 |issue= 9 |pages= 2129–2137 |year= 2007 |pmid= 17495961 |doi= 10.1038/sj.jid.5700859 |name-list-format=vanc| author2=Johansen C | author3=Rasmussen MK | display-authors=3 | last4=Funding | first4=Anne T | last5=Otkjaer | first5=Kristian | last6=Kjellerup | first6=Rasmus B | last7=Kragballe | first7=Knud | last8=Iversen | first8=Lars }} | |||
}} | |||
{{refend}} | |||
{{Serine/threonine-specific protein kinases}} | |||
{{Enzymes}} | |||
{{Portal bar|Molecular and Cellular Biology|border=no}} | |||
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[[Category:EC 2.7.11]] | |||
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
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Wikidata | |||||||
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Ribosomal protein S6 kinase alpha-4 is an enzyme that in humans is encoded by the RPS6KA4 gene.[1][2][3]
Function
This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including CREB1 and c-Fos. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.[3]
Interactions
RPS6KA4 has been shown to interact with MAPK14.[1]
References
- ↑ 1.0 1.1 Pierrat B, Correia JS, Mary JL, Tomas-Zuber M, Lesslauer W (Dec 1998). "RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)". J Biol Chem. 273 (45): 29661–29671. doi:10.1074/jbc.273.45.29661. PMID 9792677.
- ↑ Deak M, Clifton AD, Lucocq LM, Alessi DR (Sep 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): 4426–4441. doi:10.1093/emboj/17.15.4426. PMC 1170775. PMID 9687510.
- ↑ 3.0 3.1 "Entrez Gene: RPS6KA4 ribosomal protein S6 kinase, 90kDa, polypeptide 4".
Further reading
- 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): 959–963. doi:10.1126/science.273.5277.959. PMID 8688081.
- Du K, Montminy M (1999). "CREB is a regulatory target for the protein kinase Akt/PKB". J. Biol. Chem. 273 (49): 32377–32379. doi:10.1074/jbc.273.49.32377. PMID 9829964.
- Tomás-Zuber M, Mary JL, Lesslauer W (2000). "Control sites of ribosomal S6 kinase B and persistent activation through tumor necrosis factor". J. Biol. Chem. 275 (31): 23549–23558. doi:10.1074/jbc.M002586200. PMID 10806207.
- Tomás-Zuber M, Mary JL, Lamour F, et al. (2001). "C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB)". J. Biol. Chem. 276 (8): 5892–5899. doi:10.1074/jbc.M005822200. PMID 11035004.
- 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): 6324–6333. doi:10.1038/sj.onc.1204007. PMID 11175347.
- Prymakowska-Bosak M, Misteli T, Herrera JE, et al. (2001). "Mitotic phosphorylation prevents the binding of HMGN proteins to chromatin". Mol. Cell. Biol. 21 (15): 5169–5178. doi:10.1128/MCB.21.15.5169-5178.2001. PMC 87241. PMID 11438671.
- 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): 2871–2881. doi:10.1128/MCB.22.8.2871-2881.2002. PMC 133730. PMID 11909979.
- Soloaga A, Thomson S, Wiggin GR, et al. (2003). "MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14". EMBO J. 22 (11): 2788–2797. doi:10.1093/emboj/cdg273. PMC 156769. PMID 12773393.
- Wissing J, Jänsch L, Nimtz M, et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Mol. Cell. Proteomics. 6 (3): 537–547. doi:10.1074/mcp.T600062-MCP200. PMID 17192257.
- Gesser B, Johansen C, Rasmussen MK, et al. (2007). "Dimethylfumarate specifically inhibits the mitogen and stress-activated kinases 1 and 2 (MSK1/2): possible role for its anti-psoriatic effect". J. Invest. Dermatol. 127 (9): 2129–2137. doi:10.1038/sj.jid.5700859. PMID 17495961.
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