Elongation factor-2 kinase and its newly discovered relatives

FEBS Lett. 2002 Mar 6;514(1):26-9. doi: 10.1016/s0014-5793(02)02299-8.


Phosphorylation of elongation factor-2 (eEF-2) by the highly specific eEF-2 kinase results in eEF-2 inactivation and, therefore, may regulate the global rate of protein synthesis in animal cells. Cloning and sequencing of eEF-2 kinase led to the discovery of a new family of protein kinases, named alpha-kinases, whose catalytic domains display no sequence homology to conventional eukaryotic protein kinases. Several mammalian alpha-kinases have recently been cloned. Two of these alpha-kinases, named channel-kinases 1 and 2 (ChaK1 and ChaK2) represent a new type of signaling molecules that are protein kinases fused to ion channels.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / classification
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Elongation Factor 2 Kinase
  • Hydrogen-Ion Concentration
  • Mammals
  • Peptide Elongation Factor 2 / metabolism
  • Phosphorylation
  • Phylogeny


  • Peptide Elongation Factor 2
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Elongation Factor 2 Kinase