Elongation Factor 2 Kinase

Our interests in eEF-2K are the following:

Regulation of eEF-2K: We are studying precisely how eEF-2K is activated and regulated. This information is critical to understanding its contributions to both normal cellular processes and in the etiology and progression of disease states. Toward this goal, we recently identified calmodulin-stimulated autophosphorylation on a specific residue, T348, as being the key step in the activation of eEF-2K and showed that phosphorylation of S500 potentiates the activation of eEF-2K by Ca-CaM.


Domain organization of eEF-2K. The N-terminus of eEF-2K (1-725, 82.2 kDa) comprises of a CaM binding domain (CBD, dark orange), and a catalytic kinase domain (KD, light blue). Autophosphorylation on T348 comprises a key step in the activation of eEF-2K. The C-terminus comprises of three predicted SEL1-like repeats (SLRs, purple). The disordered R-loop (located between the KD and SLRs) contains several phosphorylation sites including T348 and a regulatory site, S500.