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MAPK15  -  mitogen-activated protein kinase 15

Homo sapiens

Synonyms: ERK-7, ERK-8, ERK7, ERK8, Extracellular signal-regulated kinase 7, ...
 
 
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Disease relevance of MAPK15

  • ERK8 (extracellular-signal-regulated protein kinase 8) expressed in Escherichia coli or insect cells was catalytically active and phosphorylated at both residues of the Thr-Glu-Tyr motif [1].
  • Loss of ERK7 was correlated with breast cancer progression, and all ER alpha-positive breast tumors had decreased ERK7 expression compared to that found in normal breast tissue [2].
 

High impact information on MAPK15

 

Biological context of MAPK15

 

Anatomical context of MAPK15

  • 3. Expression of ERK8 in COS cells and bacteria indicates that, in contrast to constitutively active ERK7, ERK8 has minimal basal kinase activity and a unique substrate profile [5].
  • Knockdown of endogenous ERK8 in human airway epithelial cells enhanced dexamethasone-stimulated transcriptional activity of endogenous GR [4].
 

Associations of MAPK15 with chemical compounds

  • Wild-type ERK8 expressed in HEK-293 cells was over 100-fold less active than the enzyme expressed in bacteria or insect cells, but activity could be increased by exposure to hydrogen peroxide, by incubation with the protein serine/threonine phosphatase inhibitor okadaic acid, or more weakly by osmotic shock [1].
 

Regulatory relationships of MAPK15

  • Addition of 10 nM ET-1 stimulated MAPK 15-fold within 5 min at 37 degrees C (1.08 +/- 0.02 nmoles Pi/mg/min) [6].
 

Other interactions of MAPK15

  • ERK8, which contains two SH3-binding motifs in its C-terminal region, associates with the c-Src SH3 domain in vitro and co-immunoprecipitates with c-Src in vivo [5].
 

Analytical, diagnostic and therapeutic context of MAPK15

  • The interaction between CLIC3 and ERK7 in mammalian cells was confirmed by co-immunoprecipitation [7].
  • Although EhMAPK bears good homology and phylogenetic closeness with human ERK8 and rat ERK7, sequence analysis indicates that they may be functionally different [8].

References

  1. Characterization of the reversible phosphorylation and activation of ERK8. Klevernic, I.V., Stafford, M.J., Morrice, N., Peggie, M., Morton, S., Cohen, P. Biochem. J. (2006) [Pubmed]
  2. Extracellular signal-regulated kinase 7, a regulator of hormone-dependent estrogen receptor destruction. Henrich, L.M., Smith, J.A., Kitt, D., Errington, T.M., Nguyen, B., Traish, A.M., Lannigan, D.A. Mol. Cell. Biol. (2003) [Pubmed]
  3. Activation of the Erk8 mitogen-activated protein (MAP) kinase by RET/PTC3, a constitutively active form of the RET proto-oncogene. Iavarone, C., Acunzo, M., Carlomagno, F., Catania, A., Melillo, R.M., Carlomagno, S.M., Santoro, M., Chiariello, M. J. Biol. Chem. (2006) [Pubmed]
  4. ERK8 down-regulates transactivation of the glucocorticoid receptor through Hic-5. Saelzler, M.P., Spackman, C.C., Liu, Y., Martinez, L.C., Harris, J.P., Abe, M.K. J. Biol. Chem. (2006) [Pubmed]
  5. ERK8, a new member of the mitogen-activated protein kinase family. Abe, M.K., Saelzler, M.P., Espinosa, R., Kahle, K.T., Hershenson, M.B., Le Beau, M.M., Rosner, M.R. J. Biol. Chem. (2002) [Pubmed]
  6. Endothelin and isoproterenol counter-regulate cAMP and mitogen-activated protein kinases. Wu-Wong, J.R., Opgenorth, T.J. J. Cardiovasc. Pharmacol. (1998) [Pubmed]
  7. Molecular cloning and characterization of a mitogen-activated protein kinase-associated intracellular chloride channel. Qian, Z., Okuhara, D., Abe, M.K., Rosner, M.R. J. Biol. Chem. (1999) [Pubmed]
  8. Identification, structure, and phylogenetic relationships of a mitogen-activated protein kinase homologue from the parasitic protist Entamoeba histolytica. Ray, D., Dutta, S., Banerjee, S., Banerjee, R., Raha, S. Gene (2005) [Pubmed]
 
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