Anti-eEF2K: Rabbit eEF2K Antibody

BACKGROUND Ribosomal protein synthesis is one of the oldest and best-conserved processes taking place in a living cell. Amino acid residues are added to the growing peptide chain in the ribosome by an elongation process that involves two GTP-switched elongation factors, denominated EF1 and EF2 in eukaryotes.  eEF2 (eukaryotic translation elongation factor 2) is a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. eEF2 is phosphorylated and inhibited by eEF2K. eEF2K 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) at Thr56 and Thr58, which results in the inactivation of eEF2 by causing a structural alteration that reduces its affinity for the ribosome, thereby preventing its ability to catalyze translocation.¹ eEF2 kinase is also subjected to regulation by phosphorylation, and a number of phosphorylation sites have been identified that lead to subsequent activation or inhibition of activity.^2,3 The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.

 

REFERENCES  

1. Redpath, N.T. et al: Eur. J. Biochem. 213:689-99, 1993
2. Knebel, A. et al: EMBO J. 20:4360-9, 2001
3. Rose, A.J. et al: J. Physiol. 587:1547-63, 2009