Biology:Mitogen-activated protein kinase 9

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.[1]

Function

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.[2]

Interactions

Mitogen-activated protein kinase 9 has been shown to interact with:

References

  1. "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation". Genes & Development 8 (24): 2996–3007. Dec 1994. doi:10.1101/gad.8.24.2996. PMID 8001819. 
  2. "Entrez Gene: MAPK9 mitogen-activated protein kinase 9". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5601. 
  3. "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth & Differentiation 6 (12): 1651–8. Dec 1995. PMID 9019171. 
  4. "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". The Journal of Biological Chemistry 270 (32): 18871–4. Aug 1995. doi:10.1074/jbc.270.32.18871. PMID 7642542. 
  5. 5.0 5.1 "The JIP group of mitogen-activated protein kinase scaffold proteins". Molecular and Cellular Biology 19 (10): 7245–54. Oct 1999. doi:10.1128/mcb.19.10.7245. PMID 10490659. 
  6. "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science 281 (5383): 1671–4. Sep 1998. doi:10.1126/science.281.5383.1671. PMID 9733513. Bibcode1998Sci...281.1671W. 
  7. "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway". Molecular and Cellular Biology 19 (11): 7539–48. Nov 1999. doi:10.1128/mcb.19.11.7539. PMID 10523642. 
  8. "Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3". Molecular and Cellular Biology 20 (3): 1030–43. Feb 2000. doi:10.1128/mcb.20.3.1030-1043.2000. PMID 10629060. 
  9. "JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases". Oncogene 15 (19): 2277–87. Nov 1997. doi:10.1038/sj.onc.1201401. PMID 9393873. 
  10. "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". The Journal of Biological Chemistry 277 (50): 47991–8001. Dec 2002. doi:10.1074/jbc.M202630200. PMID 12384512. 
  11. "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry 277 (40): 37783–7. Oct 2002. doi:10.1074/jbc.M204506200. PMID 12151396. 

Further reading

External links

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