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Map2k2  -  mitogen activated protein kinase kinase 2

Rattus norvegicus

Synonyms: Dual specificity mitogen-activated protein kinase kinase 2, ERK activator kinase 2, MAP kinase kinase 2, MAPK/ERK kinase 2, MAPKK 2, ...
 
 
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Disease relevance of Map2k2

 

High impact information on Map2k2

  • Consistent with this observation, we observed that MEK2, which lacks a phosphorylation site at the corresponding position, was activated only transiently following serum stimulation [2].
  • Moreover, these two growth factor-related sequential signaling events involved successively activation of MEK2-ERK2 and then MEK1/2-ERK1/2 isoforms [3].
  • Incubation with PD 98059 blocked angiotensin II (AII)-dependent phosphorylation and enzymatic activity of both MEK1 and MEK2 isoforms, leading to inhibition of the phosphorylation and activation of p44(mapk) and p42(mapk) [4].
  • The negative forms of CREB and c-Fos inhibited neurite outgrowth mediated by NCAM, arachidonic acid, dBcAMP, or MEK2 [5].
  • PC12-E2 cells were transiently transfected with expression plasmids encoding cytNCAM-140, cytNCAM-180, the constitutively active form of the mitogen-activated protein (MAP) kinase/extracellular signal-regulated kinase kinase (MEK2), and the enhanced variant of the green fluorescent protein (EGFP) [6].
 

Biological context of Map2k2

  • PC12-E2 cells were transiently transfected with expression plasmids encoding wild-type or dominant negative forms of CREB and c-Fos or an activated form of the MAPK kinase, MEK2 [5].
  • In search of antiinflammatory drugs with a new mechanism of action, U0126 was found to functionally antagonize AP-1 transcriptional activity via noncompetitive inhibition of the dual specificity kinase MEK with an IC50 of 0.07 microM for MEK 1 and 0.06 microM for MEK 2 [7].
 

Anatomical context of Map2k2

 

Associations of Map2k2 with chemical compounds

 

Other interactions of Map2k2

 

Analytical, diagnostic and therapeutic context of Map2k2

References

  1. Identification of genes related to invasion and metastasis in pancreatic cancer by cDNA representational difference analysis. Ishikawa, S., Egami, H., Kurizaki, T., Akagi, J., Tamori, Y., Yoshida, N., Tan, X., Hayashi, N., Ogawa, M. J. Exp. Clin. Cancer Res. (2003) [Pubmed]
  2. A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function. Catling, A.D., Schaeffer, H.J., Reuter, C.W., Reddy, G.R., Weber, M.J. Mol. Cell. Biol. (1995) [Pubmed]
  3. Mechanism in the sequential control of cell morphology and S phase entry by epidermal growth factor involves distinct MEK/ERK activations. Rescan, C., Coutant, A., Talarmin, H., Theret, N., Glaise, D., Guguen-Guillouzo, C., Baffet, G. Mol. Biol. Cell (2001) [Pubmed]
  4. Inhibition of growth factor-induced protein synthesis by a selective MEK inhibitor in aortic smooth muscle cells. Servant, M.J., Giasson, E., Meloche, S. J. Biol. Chem. (1996) [Pubmed]
  5. The transcription factors CREB and c-Fos play key roles in NCAM-mediated neuritogenesis in PC12-E2 cells. Jessen, U., Novitskaya, V., Pedersen, N., Serup, P., Berezin, V., Bock, E. J. Neurochem. (2001) [Pubmed]
  6. Identification of an amino acid sequence motif in the cytoplasmic domain of the NCAM-140 kDa isoform essential for its neuritogenic activity. Kolkova, K., Pedersen, N., Berezin, V., Bock, E. J. Neurochem. (2000) [Pubmed]
  7. MEK inhibitors: the chemistry and biological activity of U0126, its analogs, and cyclization products. Duncia, J.V., Santella, J.B., Higley, C.A., Pitts, W.J., Wityak, J., Frietze, W.E., Rankin, F.W., Sun, J.H., Earl, R.A., Tabaka, A.C., Teleha, C.A., Blom, K.F., Favata, M.F., Manos, E.J., Daulerio, A.J., Stradley, D.A., Horiuchi, K., Copeland, R.A., Scherle, P.A., Trzaskos, J.M., Magolda, R.L., Trainor, G.L., Wexler, R.R., Hobbs, F.W., Olson, R.E. Bioorg. Med. Chem. Lett. (1998) [Pubmed]
  8. Mitogen-activated protein kinase translocates to the nucleus during ischaemia and is activated during reperfusion. Mizukami, Y., Yoshida, K. Biochem. J. (1997) [Pubmed]
  9. PDGF-BB-mediated activation of p42(MAPK) is independent of PDGF beta-receptor tyrosine phosphorylation. Cartel, N.J., Liu, J., Wang, J., Post, M. Am. J. Physiol. Lung Cell Mol. Physiol. (2001) [Pubmed]
  10. Activation of MAP kinase kinase (MEK) and Ras by cholecystokinin in rat pancreatic acini. Duan, R.D., Zheng, C.F., Guan, K.L., Williams, J.A. Am. J. Physiol. (1995) [Pubmed]
 
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