Kinase Subfamily eEF2K

Kinase Classification: Group PKL: Family Alpha: Subfamily eEF2K

Domain Structure

eEF2K has an alpha kinase domain flanked by an N-terminal calmodulin-binding domain and a C-terminal eEF2 binding domain.

Evolution

eEF2K is found in most unikonts, though lost in fungi and insects. In fungi, it's role in phosphorylating T56 and T58 of eE2F may be taken over by the fungal-specific CAMK kinase, Rck2 [1].

Functions

eE2FK phosphorylates eukaryotic elongation factor 2 and inhibits protein synthesis. It appears to integrate multiple signals. It contains a large number of phosphorylation sites that include targets of AMPK, p38 and RSK family kinases, and is also regulated by Calcium.

References

1. Teige M, Scheikl E, Reiser V, Ruis H, and Ammerer G. Rck2, a member of the calmodulin-protein kinase family, links protein synthesis to high osmolarity MAP kinase signaling in budding yeast. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5625-30. DOI:10.1073/pnas.091610798 |