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mapk1  -  mitogen-activated protein kinase 1

Xenopus (Silurana) tropicalis

Synonyms: erk, erk2, ert1, mapk, mapk2, ...
 
 
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High impact information on mapk1

  • Before fertilization, vertebrate eggs are arrested in metaphase of meiosis II by cytostatic factor (CSF), an activity that requires activation of the mitogen-activated protein kinase (MAPK) pathway [1].
  • Persistent activation of p42 mitogen-activated protein kinase (p42 MAPK) during mitosis induces a "cytostatic factor" arrest, the arrest responsible for preventing the parthenogenetic activation of unfertilized eggs [2].
  • Thus, Rsk appears to be the mediator of MAPK-dependent CSF arrest in vertebrate unfertilized eggs [1].
  • Analysis of individual oocytes showed that the response of MAPK to progesterone or Mos was equivalent to that of a cooperative enzyme with a Hill coefficient of at least 35, more than 10 times the Hill coefficient for the binding of oxygen to hemoglobin [3].
  • Interference with MAPK activation by immunodepletion of its activator MEK, or by addition of the MEK inhibitor PD98059, caused precocious termination of mitosis and interfered with production of normal mitotic microtubules [4].
 

Biological context of mapk1

 

Anatomical context of mapk1

  • Moreover, the expression of MAPK phosphatase-1 (MKP-1, also called CL100) blocks the growth factor-stimulated mesoderm induction [5].
  • Ectodermal MAPK activity increased between late blastula and midgastrula stages [9].
  • Although induction of posterior neural ectoderm by FGF was accompanied by an elevation of MAPK activity, relative MAPK activity associated with posterior neural fate was no higher than that of ectoderm specified to adopt an anterior neural fate [9].
  • Reconstitution of p21ras-dependent and -independent mitogen-activated protein kinase activation in a cell-free system [10].
  • Likewise, the dephosphorylation and inactivation of p42 MAPK are critical for the progression of fertilized eggs out of meiosis and through the first mitotic cell cycle [11].
 

Associations of mapk1 with chemical compounds

 

Other interactions of mapk1

 

Analytical, diagnostic and therapeutic context of mapk1

References

  1. Induction of metaphase arrest in cleaving Xenopus embryos by the protein kinase p90Rsk. Gross, S.D., Schwab, M.S., Lewellyn, A.L., Maller, J.L. Science (1999) [Pubmed]
  2. The protein kinase p90 rsk as an essential mediator of cytostatic factor activity. Bhatt, R.R., Ferrell, J.E. Science (1999) [Pubmed]
  3. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Ferrell, J.E., Machleder, E.M. Science (1998) [Pubmed]
  4. Requirement for MAPK activation for normal mitotic progression in Xenopus egg extracts. Guadagno, T.M., Ferrell, J.E. Science (1998) [Pubmed]
  5. Involvement of the MAP kinase cascade in Xenopus mesoderm induction. Gotoh, Y., Masuyama, N., Suzuki, A., Ueno, N., Nishida, E. EMBO J. (1995) [Pubmed]
  6. The alpha subunit of the human granulocyte-macrophage colony-stimulating factor receptor signals for glucose transport via a phosphorylation-independent pathway. Ding, D.X., Rivas, C.I., Heaney, M.L., Raines, M.A., Vera, J.C., Golde, D.W. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  7. A developmental timer regulates degradation of cyclin E1 at the midblastula transition during Xenopus embryogenesis. Howe, J.A., Newport, J.W. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Oncogenic ras triggers the activation of 42-kDa mitogen-activated protein kinase in extracts of quiescent Xenopus oocytes. Shibuya, E.K., Polverino, A.J., Chang, E., Wigler, M., Ruderman, J.V. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  9. Mitogen-activated protein kinase and neural specification in Xenopus. Uzgare, A.R., Uzman, J.A., El-Hodiri, H.M., Sater, A.K. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  10. Reconstitution of p21ras-dependent and -independent mitogen-activated protein kinase activation in a cell-free system. VanRenterghem, B., Gibbs, J.B., Maller, J.L. J. Biol. Chem. (1993) [Pubmed]
  11. Distinct, constitutively active MAPK phosphatases function in Xenopus oocytes: implications for p42 MAPK regulation In vivo. Sohaskey, M.L., Ferrell, J.E. Mol. Biol. Cell (1999) [Pubmed]
  12. The antibiotic azatyrosine suppresses progesterone or [Val12]p21 Ha-ras/insulin-like growth factor I-induced germinal vesicle breakdown and tyrosine phosphorylation of Xenopus mitogen-activated protein kinase in oocytes. Campa, M.J., Glickman, J.F., Yamamoto, K., Chang, K.J. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  13. Activation of p42 mitogen-activated protein kinase (MAPK), but not c-Jun NH(2)-terminal kinase, induces phosphorylation and stabilization of MAPK phosphatase XCL100 in Xenopus oocytes. Sohaskey, M.L., Ferrell, J.E. Mol. Biol. Cell (2002) [Pubmed]
  14. The polo-like kinase Plx1 is required for activation of the phosphatase Cdc25C and cyclin B-Cdc2 in Xenopus oocytes. Qian, Y.W., Erikson, E., Taieb, F.E., Maller, J.L. Mol. Biol. Cell (2001) [Pubmed]
  15. Regulation of Na(+) reabsorption by the aldosterone-induced small G protein K-Ras2A. Stockand, J.D., Spier, B.J., Worrell, R.T., Yue, G., Al-Baldawi, N., Eaton, D.C. J. Biol. Chem. (1999) [Pubmed]
  16. Mutant of insulin receptor substrate-1 incapable of activating phosphatidylinositol 3-kinase did not mediate insulin-stimulated maturation of Xenopus laevis oocytes. Yamamoto-Honda, R., Honda, Z., Ueki, K., Tobe, K., Kaburagi, Y., Takahashi, Y., Tamemoto, H., Suzuki, T., Itoh, K., Akanuma, Y., Yazaki, Y., Kadowaki, T. J. Biol. Chem. (1996) [Pubmed]
  17. The casein kinase II beta subunit binds to Mos and inhibits Mos activity. Chen, M., Li, D., Krebs, E.G., Cooper, J.A. Mol. Cell. Biol. (1997) [Pubmed]
  18. Regulation of melanosome movement by MAP kinase. Andersson, T.P., Svensson, S.P., Karlsson, A.M. Pigment Cell Res. (2003) [Pubmed]
  19. The MAP kinase cascade: its role in Xenopus oocytes, eggs and embryos. Gotoh, Y., Nishida, E. Progress in cell cycle research. (1995) [Pubmed]
  20. Deregulation of mitogen-activated protein kinase at low pH due to a structural rearrangement of activation segment. Tokmakov, A.A., Sato, K.I., Fukami, Y. Biochim. Biophys. Acta (2000) [Pubmed]
 
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