Eukaryotic elongation factor-2 kinase (eEF-2 kinase), also known as calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase (CaMKIII) is an enzyme that in humans is encoded by the EEF2Kgene.
eEF-2 kinase is a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links activation of cell surface receptors to cell division. This kinase is involved in the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function. The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.
^Leprivier G, Remke M, Rotblat B, Dubuc A, Mateo AR, Kool M, Agnihotri S, El-Naggar A, Yu B, Somasekharan SP, Faubert B, Bridon G, Tognon CE, Mathers J, Thomas R, Li A, Barokas A, Kwok B, Bowden M, Smith S, Wu X, Korshunov A, Hielscher T, Northcott PA, Galpin JD, Ahern CA, Wang Y, McCabe MG, Collins VP, Jones RG, Pollak M, Delattre O, Gleave ME, Jan E, Pfister SM, Proud CG, Derry WB, Taylor MD, Sorensen PH (May 2013). "The eEF2 kinase confers resistance to nutrient deprivation by blocking translation elongation". Cell153 (5): 1064–79. doi:10.1016/j.cell.2013.04.055. PMID23706743.
Nairn AC, Palfrey HC (1988). "Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2". J. Biol. Chem.262 (36): 17299–303. PMID3693353.
Arora S, Yang JM, Craft J, Hait W (2002). "Detection of anti-elongation factor 2 kinase (calmodulin-dependent protein kinase III) antibodies in patients with systemic lupus erythematosus". Biochem. Biophys. Res. Commun.293 (3): 1073–6. doi:10.1016/S0006-291X(02)00324-8. PMID12051769.
Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis.8: 205–20. PMID12107410.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet.36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Browne GJ, Finn SG, Proud CG (2004). "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". J. Biol. Chem.279 (13): 12220–31. doi:10.1074/jbc.M309773200. PMID14709557.
Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Anal. Chem.76 (10): 2763–72. doi:10.1021/ac035352d. PMID15144186.
Li X, Alafuzoff I, Soininen H, et al. (2005). "Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain". FEBS J.272 (16): 4211–20. doi:10.1111/j.1742-4658.2005.04833.x. PMID16098202.
Hait WN, Wu H, Jin S, Yang JM (2007). "Elongation factor-2 kinase: its role in protein synthesis and autophagy". Autophagy2 (4): 294–6. PMID16921268.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol.24 (10): 1285–92. doi:10.1038/nbt1240. PMID16964243.