Eukaryotic elongation factor 2 kinase activity is controlled by multiple inputs from oncogenic signaling.

@article{Wang2014EukaryoticEF,
  title={Eukaryotic elongation factor 2 kinase activity is controlled by multiple inputs from oncogenic signaling.},
  author={Xuemin Wang and Sergio Regufe da Mota and Rui Liu and Claire E. J. Moore and Jianling Xie and Francesco Lanucara and Usha Agarwala and S{\'e}bastien Pyr Dit Ruys and Didier Vertommen and Mark H. Rider and Claire E Eyers and Christopher G Proud},
  journal={Molecular and cellular biology},
  year={2014},
  volume={34 22},
  pages={
          4088-103
        }
}
Eukaryotic elongation factor 2 kinase (eEF2K), an atypical calmodulin-dependent protein kinase, phosphorylates and inhibits eEF2, slowing down translation elongation. eEF2K contains an N-terminal catalytic domain, a C-terminal α-helical region and a linker containing several regulatory phosphorylation sites. eEF2K is expressed at high levels in certain cancers, where it may act to help cell survival, e.g., during nutrient starvation. However, it is a negative regulator of protein synthesis and… CONTINUE READING
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