Elongation factor-2 kinase: effective inhibition by the novel protein kinase inhibitor rottlerin and relative insensitivity towards staurosporine

FEBS Lett. 1994 Jan 24;338(1):85-8. doi: 10.1016/0014-5793(94)80121-5.


The elongation factor-2 (eEF-2) is selectively phosphorylated by the eEF-2 kinase (calmodulin-dependent kinase III). This phosphorylation can be inhibited by calmodulin antagonists, such as CGS 9343B (IC50 = 4 microM). The novel protein kinase inhibitor rottlerin is shown to suppress eEF-2 phosphorylation with an IC50 of 5.3 microM. By contrast, the eEF-2 kinase is rather resistant towards the potent but non-selective protein kinase inhibitor staurosporine (IC50 > 50 microM) and thus can be differentiated from most other protein kinases that are suppressed by staurosporine in the nM range.

MeSH terms

  • Acetophenones / pharmacology*
  • Alkaloids / pharmacology*
  • Animals
  • Benzopyrans / pharmacology*
  • Calcium-Calmodulin-Dependent Protein Kinases / antagonists & inhibitors*
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Mice
  • Phosphorylation
  • Protein Kinase Inhibitors*
  • Staurosporine


  • Acetophenones
  • Alkaloids
  • Benzopyrans
  • Protein Kinase Inhibitors
  • rottlerin
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Staurosporine