eEF2K controls the elongation stage of protein synthesis and is regulated by many different inputs. We are studying its role in normal cell physiology and in disease states such as cancer.
Eukaryotic elongation factor 2 kinase (eEF2K) phosphorylates and inactivates eEF2, the protein which mediates ribosomal translocation during elongation of the new polypeptide chain.
We are interested in eEF2K for several reasons. First, it is a very unusual protein kinase that belongs to a small family of kinases distinct from the main kinase superfamily. We are working to elucidate its structure and control, using a range of biophysical and structural approaches.
Second, the activity and expression levels of eEF2K are tightly controlled by many signalling pathways, including mTOR. We are investigating how these control mechanisms operate and their importance for regulating protein synthesis in a wide range of settings.
Thirdly, the fact that eEF2K is so tightly regulated implies it lays important role in controlling protein synthesis, and we are studying several aspects of this, e.g., its role in cancer cells, its function in heart and muscle physiology, and its role in controlling synaptic protein synthesis during learning and memory consolidation.
Funding: Wellcome Trust, Cancer Research UK, British Heart Foundation, BBSRC