Eukaryotic elongation factor-2 kinase (eEF-2k) previously known as Ca2+/calmodulin-dependent protein kinase III, is an abundant cytoplasmic protein highly specific for elongation factor-2 (eEf-2) (1). Phosphorylation of eEF-2 by eEF-2 kinase on specific threonine residues results in the inactivation of eEF-2 and in termination of mRNA translation (2). The activity of eEF2 kinase is not only dependent upon Ca2+ ions, calmodulin (CaM) and insulin, but is also regulated both negatively and positively via phosphorylation by different protein kinases (AMPK, S6K1, p90 RSK) (3-4). There is also evidence that eEF-2 phosphorylation is involved in the regulation of cell cycle progression, cellular differentiation, oogensis and malignant tumors (5-6).
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