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Gene Review

Eef2k  -  eukaryotic elongation factor-2 kinase

Rattus norvegicus

Synonyms: Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, Eukaryotic elongation factor 2 kinase, eEF-2 kinase, eEF-2K
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High impact information on Eef2k


Biological context of Eef2k

  • Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398 [6].
  • We have recently shown that eEF2 kinase is also controlled by phosphorylation by AMP-activated protein kinase (AMPK), a key regulator of cellular energy homeostasis [3].

Anatomical context of Eef2k

  • We have studied angiotensin II (ANG II)-dependent regulation of eukaryotic elongation factor-2 (eEF-2), an essential component of protein translation required for polypeptide elongation, in rat neonatal cardiac myocytes. eEF2 is fully active in its dephosphorylated state and is inhibited following phosphorylation by eEF2 kinase [7].

Associations of Eef2k with chemical compounds


Regulatory relationships of Eef2k


Other interactions of Eef2k


Analytical, diagnostic and therapeutic context of Eef2k

  • Northern blot analysis demonstrated that eEF-2K mRNA is expressed in a number of different tissues and that it may exist in multiple forms [5].


  1. Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase. Ryazanov, A.G., Ward, M.D., Mendola, C.E., Pavur, K.S., Dorovkov, M.V., Wiedmann, M., Erdjument-Bromage, H., Tempst, P., Parmer, T.G., Prostko, C.R., Germino, F.J., Hait, W.N. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. AMP-activated protein kinase protects cardiomyocytes against hypoxic injury through attenuation of endoplasmic reticulum stress. Terai, K., Hiramoto, Y., Masaki, M., Sugiyama, S., Kuroda, T., Hori, M., Kawase, I., Hirota, H. Mol. Cell. Biol. (2005) [Pubmed]
  3. Activation of AMP-activated protein kinase inhibits protein synthesis associated with hypertrophy in the cardiac myocyte. Chan, A.Y., Soltys, C.L., Young, M.E., Proud, C.G., Dyck, J.R. J. Biol. Chem. (2004) [Pubmed]
  4. Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis. Horman, S., Browne, G., Krause, U., Patel, J., Vertommen, D., Bertrand, L., Lavoinne, A., Hue, L., Proud, C., Rider, M. Curr. Biol. (2002) [Pubmed]
  5. Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase. Redpath, N.T., Price, N.T., Proud, C.G. J. Biol. Chem. (1996) [Pubmed]
  6. Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398. Browne, G.J., Finn, S.G., Proud, C.G. J. Biol. Chem. (2004) [Pubmed]
  7. Angiotensin II regulates phosphorylation of translation elongation factor-2 in cardiac myocytes. Everett, A.D., Stoops, T.D., Nairn, A.C., Brautigan, D. Am. J. Physiol. Heart Circ. Physiol. (2001) [Pubmed]
  8. Regulation of translation elongation and phosphorylation of eEF2 in rat pancreatic acini. Sans, M.D., Xie, Q., Williams, J.A. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  9. Enhancement of translation elongation in neurons by brain-derived neurotrophic factor: implications for mammalian target of rapamycin signaling. Inamura, N., Nawa, H., Takei, N. J. Neurochem. (2005) [Pubmed]
  10. Activation of mRNA translation in rat cardiac myocytes by insulin involves multiple rapamycin-sensitive steps. Wang, L., Wang, X., Proud, C.G. Am. J. Physiol. Heart Circ. Physiol. (2000) [Pubmed]
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