Mitogen-activated protein kinase 9

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Mitogen-activated protein kinase 9
Identifiers
Symbols MAPK9 ; JNK-55; JNK2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; PRKM9; p54aSAPK
External IDs Template:OMIM5 Template:MGI HomoloGene: 55685
RNA expression pattern
File:PBB GE MAPK9 203218 at tn.png
File:PBB GE MAPK9 210570 x at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Mitogen-activated protein kinase 9, also known as MAPK9, is a human gene.

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.[1]

References

  1. ↑ "Entrez Gene: MAPK9 mitogen-activated protein kinase 9".

Further reading

  • Davis RJ (2000). "Signal transduction by the JNK group of MAP kinases". Cell. 103 (2): 239–52. PMID 11057897.
  • Freedman BD, Liu QH, Del Corno M, Collman RG (2004). "HIV-1 gp120 chemokine receptor-mediated signaling in human macrophages". Immunol. Res. 27 (2–3): 261–76. PMID 12857973.
  • Lee C, Liu QH, Tomkowicz B; et al. (2004). "Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways". J. Leukoc. Biol. 74 (5): 676–82. doi:10.1189/jlb.0503206. PMID 12960231.
  • Denys H, Desmet R, Stragier M; et al. (1978). "Cystitis emphysematosa". Acta urologica Belgica. 45 (4): 327–31. PMID 602896.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151.
  • Livingstone C, Patel G, Jones N (1995). "ATF-2 contains a phosphorylation-dependent transcriptional activation domain". EMBO J. 14 (8): 1785–97. PMID 7737129.
  • Sluss HK, Barrett T, Dérijard B, Davis RJ (1994). "Signal transduction by tumor necrosis factor mediated by JNK protein kinases". Mol. Cell. Biol. 14 (12): 8376–84. PMID 7969172.
  • Kallunki T, Su B, Tsigelny I; et al. (1995). "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation". Genes Dev. 8 (24): 2996–3007. PMID 8001819.
  • Gille H, Strahl T, Shaw PE (1996). "Activation of ternary complex factor Elk-1 by stress-activated protein kinases". Curr. Biol. 5 (10): 1191–200. PMID 8548291.
  • Chu Y, Solski PA, Khosravi-Far R; et al. (1996). "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation". J. Biol. Chem. 271 (11): 6497–501. PMID 8626452.
  • Bocco JL, Bahr A, Goetz J; et al. (1996). "In vivo association of ATFa with JNK/SAP kinase activities". Oncogene. 12 (9): 1971–80. PMID 8649858.
  • Gupta S, Barrett T, Whitmarsh AJ; et al. (1996). "Selective interaction of JNK protein kinase isoforms with transcription factors". EMBO J. 15 (11): 2760–70. PMID 8654373.
  • Kallunki T, Deng T, Hibi M, Karin M (1997). "c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions". Cell. 87 (5): 929–39. PMID 8945519.
  • Jabado N, Pallier A, Jauliac S; et al. (1997). "gp160 of HIV or anti-CD4 monoclonal antibody ligation of CD4 induces inhibition of JNK and ERK-2 activities in human peripheral CD4+ T lymphocytes". Eur. J. Immunol. 27 (2): 397–404. PMID 9045910.
  • Janknecht R, Hunter T (1997). "Convergence of MAP kinase pathways on the ternary complex factor Sap-1a". EMBO J. 16 (7): 1620–7. doi:10.1093/emboj/16.7.1620. PMID 9130707.
  • 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. PMID 9155018.
  • Chow CW, Rincón M, Cavanagh J; et al. (1997). "Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway". Science. 278 (5343): 1638–41. PMID 9374467.
  • Hu MC, Qiu WR, Wang YP (1997). "JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases". Oncogene. 15 (19): 2277–87. doi:10.1038/sj.onc.1201401. PMID 9393873.
  • Lannuzel A, Barnier JV, Hery C; et al. (1998). "Human immunodeficiency virus type 1 and its coat protein gp120 induce apoptosis and activate JNK and ERK mitogen-activated protein kinases in human neurons". Ann. Neurol. 42 (6): 847–56. doi:10.1002/ana.410420605. PMID 9403476.
  • Fuchs SY, Xie B, Adler V; et al. (1998). "c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors". J. Biol. Chem. 272 (51): 32163–8. PMID 9405416.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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