Phosphorylation of elongation factor-2 kinase differentially regulates the enzyme's stability under stress conditions.

ABSTRACT: Eukaryotic elongation factor-2 kinase (eEF-2K) is a Ca(2+)/calmodulin-dependent enzyme that negatively regulates protein synthesis. eEF-2K has been shown to be up-regulated in cancer, and to play an important role in cell survival through inhibition of protein synthesis. Post-translational modification of protein synthesis machinery is important for its regulation and could be critical for survival of cancer cells encountering stress. The purpose of our study was to examine the regulation of eEF-2K during stress with a focus on the roles of phosphorylation in determining the stability of eEF-2K. We found that stress conditions (nutrient deprivation and hypoxia) increase eEF-2K protein. mRNA levels are only transiently increased and shortly return to normal, while eEF-2K protein levels cont

SUBMITTER: Huber-Keener KJ 

PROVIDER: S-EPMC3614095 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature