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Data suggest forkhead box M1 (FOXM1 (show FOXM1 Proteins))/eukaryotic elongation factor 2 kinase (eEF2K) axis as a molecular target in breast and other cancers.
These new substrates suggest that eEF2K has a more diverse role in regulating cellular energy usage that involves multiple pathways and regulatory feedback.
Myostatin (show MSTN Proteins) inhibits eEF2K-eEF2 (show EEF2 Proteins) by regulating AMPK (show PRKAA1 Proteins) to suppress protein synthesis.
The structural basis for the recognition of EEF2K by calmodulin has been presented.
eEF2K activity is increased in postmortem Alzheimer's disease (AD) patient cortex and hippocampus, and in the hippocampus of aged transgenic AD mice. eEF2K inhibition using pharmacological or genetic approaches prevented the toxic effects of Abeta42 oligomers on neuronal viability and dendrite formation in vitro. Findings highlight the potential utility of eEF2K inhibition to reduce Abeta (show APP Proteins)-mediated oxidative stress in AD.
Results demonstrated that the promotive effect of eEF-2K on glycolysis resulted from the kinase-mediated restriction of synthesis of the protein phosphatase 2A-A (PP2A (show PPP2R4 Proteins)-A).
This study reports how phosphorylation of a regulatory site (Ser-500) integrates with Ca(2+) and CaM to influence eEF-2K activity.
Article reviews recent evidence concerning the role of eEF2K in human diseases; growing evidence links eEF2K to a range of human diseases, including cardiovascular conditions (atherosclerosis, via macrophage survival) and pulmonary arterial hypertension, as well as solid tumors, where eEF2K appears to play contrasting roles depending on tumor type and stage. eEF2K is also involved in neurological disorders. [Review]
Recent evidence shows that eEF2K plays an important role in learning and memory, processes that require the synthesis of new proteins and involve Ca-mediated signalling. eEF2K is activated under conditions of nutrient and energy depletion
Results show that eEF2K is rapidly activated in response to acidosis in cells, an effect that is followed by its downregulation.
results suggest that protective versus pro-apoptotic roles of eEF2K depend on the type of cells: eEF2K is protective in highly proliferative cells, such as small intestinal stem cells and cancer cells, which are more susceptible to mitotic catastrophe.
Using an eEF2K gain-of-function design in vitro as well as eEF2K-KO mice, we show that eEF2K activity regulates the excitation/inhibition balance by downregulating vesicle release at inhibitory synapses and tonic inhibition. This translates into a reduced susceptibility of eEF2K-KO mice for seizures without major behavioral alterations with the exception of impaired contextual and trace fear memory
hese data suggest that mmu-miR (show MLXIP Proteins)-125b decreases NO production in activated macrophages at least partially by suppressing eEF2K and CCNA2 (show CCNA2 Proteins) expression.
eEF2K protects cancer cells against nutrient starvation by inhibiting protein synthesis rather than by activating autophagy.
The findings of this study suggested that eEF2K likely contributes to neuronal function by regulating the synthesis of microtubule-related proteins.
eEF2K mediates PDGF-BB-induced SMCs proliferation and migration through activating ERK, Akt, p38 and HSP27 signals in a calmodulin-dependent manner
Data show that eEF2K is activated during hypoxia or upon inhibition of prolyl hydroxylases and inhibited by its hydroxylation on a highly conserved proline residue, restricting its activity during normoxia.
data suggest that achieving an active conformation, rather than eEF2K activity per se, is required for its susceptibility to degradation.
This gene encodes a highly conserved protein kinase in the calmodulin-mediated signaling pathway that links activation of cell surface receptors to cell division. This kinase is involved in the regulation of protein synthesis. It phosphorylates eukaryotic elongation factor 2 (EEF2) and thus inhibits the EEF2 function. The activity of this kinase is increased in many cancers and may be a valid target for anti-cancer treatment.
calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
, calcium/calmodulin-dependent eukaryotic elongation factor-2 kinase
, calmodulin-dependent protein kinase III
, eEF-2 kinase
, elongation factor-2 kinase
, eukaroytic elongation factor 2 kinase
, eukaryotic elongation factor 2 kinase
, eukaryotic elongation factor-2 kinase
, eukaroytic elongation factor 2 kinase-like
, elongation factor 2 kinase