Journal
CELLULAR SIGNALLING
Volume 29, Issue -, Pages 78-83Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2016.10.006
Keywords
eEF2K; eEF2; Translation elongation; Energy homeostasis alpha4; AMPK
Categories
Funding
- Howard Hughes Medical Institute
- NIH [U19AI109622, R01AI099245]
- Biomedical Technology Research Centers program of the NIH National Institute of General Medical Sciences, NIH NIGMS [8P41GM103481]
- [P41GM103481]
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Elongation Factor-2 Kinase (eEF2K) in an unusual mammalian enzyme that has one known substrate, elongation factor-2. It belongs to a class of kinases, called alpha kinases, that has little sequence identity to the >500 conventional protein kinases, but performs the same reaction and has similar catalytic residues. The phosphorylation of eEF2 blocks translation elongation, which is thought to be critical to regulating cellular energy usage. Here we report a system for discovering new substrates of alpha kinases and identify the first new substrates of eEF2K(including AMPK and alpha4, and determine a sequence motif for the kinase that shows a requirement for threonine residues as the target of phosphorylation. These new substrates suggest that eEF2K has a more diverse role in regulating cellular energy usage that involves multiple pathways and regulatory feedback. (C) 2016 Elsevier Inc. All rights reserved.
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