Eukaryotic elongation factor 2 (eEF2) catalyzes the translocation of peptidyl-tRNA from the A site to the P site on the ribosome. eEF2 kinase (eEF2K) phosphorylates and inactivates eEF2, resulting in the inhibition of peptide-chain elongation. eEF2K is normally dependent on Ca2+ ions and calmodulin, and can be activated by PKA in response to elevated cAMP levels during cell stress- or starvation-related conditions. Regulation of eEF2K occurs through phosphorylation at multiple sites. Ser-78 phosphorylation is required for calmodulin binding and eEF2K activity, while phosphorylation of Ser-500 is required for Ca2+/calmodulin-independent kinase activity. Thr-348 is an autophosphorylation site that is required for kinase activity. Inhibitory phosphorylation may also regulate eEF2K, since phosphorylation at Ser-359 by SAPK4/p38δ causes inactivation of eEF2K. Thus, multisite phospho-regulation of eEF2K may be important for proper control of eEF2K activity and protein translation.
Smith, E.M. & Proud, C.G. (2008) EMBO J. 27(7):1005.
Ryazanov, A.G. et al. (1997) Proc Natl Acad Sci. USA. 94:4884.
*For more information, see UniProt Accession O00418
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: