eEF2K Background Information The activity of the purified eukaryotic elongation-factor-2 kinase (eEF2K) is completely dependent on calcium and calmodulin, and autophosphorylation on serine and threonine residues is calcium/calmodulin-dependent. eEF2K is a ubiquitous protein kinase that phosphorylates and inactivates eEF2, and thus can modulate the rate of polypeptide chain elongation during translation. eEF2K is detected in skeletal muscle extracts and is phosphorylated rapidly by SAPK4, but poorly by p38, p38g, JNK or ERK 2. SAPK4 phosphorylates eEF2K at Ser 359 and Ser 396 in vitro, causing its inactivation. The phosphorylation of eEF2K at Ser 359 is also induced by insulin-like growth factor-1. Ser 359 is in close proximity to Ser 366 and the Ser 366 residue also becomes phosphorylated in response to growth factors. eEF2K is phosphorylated by p70 S6 kinase at Ser 366 and this results in the inactivation of eEF2K, especially at low (micromolar) calcium concentrations.
