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Information on EC 2.7.11.20 - elongation factor 2 kinase and Organism(s) Mus musculus and UniProt Accession O08796
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2.7.11.20 elongation factor 2 kinaseIUBMB Comments
Requires Ca2+ and calmodulin for activity. The enzyme can also be phosphorylated by the catalytic subunit of EC 2.7.11.11, cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca2+ [1,2].
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Word Map
- 2.7.11.20
- rapamycin
-
perk
- starvation
- mtor
- synaptic
-
heme-regulated
- autophosphorylation
-
uncharged
- eif4e
-
pkr-like
-
ido
-
autokinase
-
alpha-kinase
-
acid-starved
-
cam-dependent
- rottlerin
- medicine
-
histidyl-trna
- pharmacology
- agriculture
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
eef2k, eef-2k, eif2alpha kinase, eef-2 kinase, eef2 kinase, eukaryotic elongation factor 2 kinase, gcn2 kinase, eukaryotic elongation factor-2 kinase, elongation factor-2 kinase, elongation factor 2 kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GCN2
additional information
-
MHCKs and eEF-2Ks comprise a distinct subgroup within the alpha kinase famiily
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[elongation factor 2] phosphotransferase
Requires Ca2+ and calmodulin for activity. The enzyme can also be phosphorylated by the catalytic subunit of EC 2.7.11.11, cAMP-dependent protein kinase. Elongation factor 2 is phosphorylated in several cell types in response to various growth factors, hormones and other stimuli that raise intracellular Ca2+ [1,2].
CAS REGISTRY NUMBER
COMMENTARY
116283-83-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
ATP + [MHCK A peptide substrate]
ADP + [MHCK A peptide substrate] phosphate
-
i.e. YAYDTRYRR
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
the enzyme phosphorylates Thr56 of eukaryotic elongation factor 2
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
the enzyme is involved in eukaryotic elongation factor 2 kinase in ER stress-induced signaling and cell death by inducing stress factors, regulation cascade, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
high glucose and high insulin regulate phosphorylation of eEF2 and eEF2 kinase by rapidly increasing activating Thr56 dephosphorylation of eEF2 and inactivating Ser366 phosphorylation of eEF2 kinase, events that facilitate elongation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
i.e. eEF2, both AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, phosphorylate eEF2, thus two distinct paths lead to eEF2 phosphorylation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the enzyme exhibits strong preference for threonine as the phosphoacceptor amino acid, substrate specificity and phosphoacceptor amino acid specificity, overview
-
-
?
additional information
?
-
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
additional information
?
-
-
a lysine or arginine in the P+1 position on the C-terminal side of the phosphoacceptor threonine, P site, is critical for peptide substrate recognition by eEF-2K, eEF-2K requires basic residues in both the P+1 and P+3 positions to recognize peptide substrates, overview
-
-
?
additional information
?
-
-
non-muscle myosin II is a poor substrate for eEF-2 kinase, while eukaryotic elongation factor 2 is no substrate of kinase TRPM7
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
the enzyme is involved in eukaryotic elongation factor 2 kinase in ER stress-induced signaling and cell death by inducing stress factors, regulation cascade, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
ATP + [eukaryotic translation initiation factor 2]
ADP + [eukaryotic translation initiation factor 2]phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
-
-
-
?
ATP + [elongation factor 2]
ADP + [elongation factor 2] phosphate
phosphorylation at Thr56
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
-
-
-
?
ATP + [eukaryotic elongation factor 2]
ADP + [eukaryotic elongation factor 2] phosphate
the enzyme phosphorylates Thr56 of eukaryotic elongation factor 2
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
-
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
eEF2 is involved in eEF2 in neurite outgrowth regulation mechanism, since phosphorylated eEF2 inhibits mRNA translation via inhibition of eEF2-ribosome binding, calcium elevation appears to inhibit mRNA translation in growth cones by a synergistic mechanism involving regulation of EF2K, S6K, and eEF2 itself, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
high glucose and high insulin regulate phosphorylation of eEF2 and eEF2 kinase by rapidly increasing activating Thr56 dephosphorylation of eEF2 and inactivating Ser366 phosphorylation of eEF2 kinase, events that facilitate elongation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase, AMPK, and eEF2 kinase, eEF2K, regulation, overview
-
-
?
ATP + [eukaryotic translation elongation factor 2]
ADP + [eukaryotic translation elongation factor 2] phosphate
-
the reaction leads to derepression of transcription factor GCN4
-
-
?
additional information
?
-
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
-
?
additional information
?
-
-
the GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of the essential amino acid leucine, thus, the enzyme acts as sensor for amino acid deficiency, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7-amino-1-cyclopropyl-3-ethyl-1,2,3,4-tetrahydro-2,4-dioxo-pyrido[2,3-d]pyrimidine-6-carboxamide
inhibits eEF2 phosphorylation in cells as well as in vitro
JAN-384
a JAN-384 highly selective eEF2K inhibitor, comparison to inhibition of other protein kinases
-
TX-1123
inhibits eEF2K, but also affects the activity of tyrosine kinases and exhibits mitochondrial toxicity
ethanol
-
decreases phosphorylation of eEF2K, whereas elongation factor 2 phosphorylation increases, but this response is not mediated by eEF2K
lopinavir
-
i.e. LPV, increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview
additional information
-
rottlerin suppresses eEF2K, but not eEF2 phosphorylation in myocytes
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bicuculline
elevation of eEF2K activity with bicuculline, a GABA receptor antagonist
D-glucose
-
high glucose or high insulin rapidly increase inactivating Ser366 phosphorylation of eEF2 kinase
Insulin
-
high glucose or high insulin rapidly increase inactivating Ser366 phosphorylation of eEF2 kinase
-
Calmodulin
required, enzyme eEF2K interacts with calmodulin (CaM) through a binding site which lies almost immediately N terminal to its catalytic domain. Comparison of human and murine CaM-binding sites, overview. Hydroxylation of Pro98 impairs binding of eEF2K to calmodulin and its activation by calmodulin
additional information
AMPK activates eEF2K via phosphorylation, which is not involved in enzyme activation in hypoxia conditions. Hypoxia or DMOG treatment enhance eEF2 phosphorylation without increasing the levels of the eEF2K protein.
-
additional information
-
inhibition of eEF2 phosphorylation leads to increased activity of its upstream regulators AMP-activated protein kinase and eEF2 kinase, overview
-
additional information
-
the enzyme is activated by uncharged tRNA-dependent mechanisms
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression of lipogenic genes and the activity of fatty acid synthase in the liver are repressed and lipid stores in adipose tissue are mobilized in GCN2 wild-type mice upon leucine deprivation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
eukaryotic elongation factor 2 kinase (eEF2K) is a member of the small group of atypical alpha-kinases, eEF2K is not a member of the main kinase superfamily. alpha-Kinases show no sequence similarity to the main protein kinase superfamily, although they do display limited three-dimensional structural similarity
malfunction
metabolism
the eEF2K protein is degraded via a proteasome-dependent pathway
physiological function
malfunction
physiological function
malfunction
eEF2K-knockout mice are viable and fertile under standard vivarium conditions. mGluR-induced long-term depression (LTD), but not LTD induced by other stimuli, is impaired in eEF2K knockout mice. The memory deficits in eEF2K knock-in mice are due to sleep-related alterations. Fear-conditioning responses in mice are deficient in eEF2K activity
malfunction
knockout of eEF2K protects mice from a lethal dose of whole-body ionizing radiation at 8 Gy by reducing apoptosis levels in both bone marrow and gastrointestinal tracts. eEF2K deficiency results in more severe damage to the gastrointestinal tract at 20 Gy with the increased mitotic cell death in small intestinal stem cells. Elevation of Akt/ERK activity as well as the reduction of p21 expression occur in Eef2k-/- cells Eef2k-/- mice display opposite sensitivities at low dose and high dose of ionizing radiation according to tissue and cell types, overview. Consistent with the role of eEF2K in apoptosis, cleaved caspase-3-positive and TUNEL-positive cells are reduced in Eef2k-deficient mice
malfunction
processes related to microtubules are particularly sensitive to eEF2K inhibition
malfunction
enzyme deficiency leads to impaired mGluR-long term potentiation, higher miniature inhibitory postsynaptic current frequency and amplitude in hippocampal granule cells, higher tonic inhibition measured in the in granule cells of the dentate gyrus, and impaired AMPAR-endocytosis following mGluR activation. The heterozygous deletion of the enzyme in mice models of Alzheimer's disease rescue cognitive, morphological and electrophysiological alterations associated to Alzheimer's disease
physiological function
eEF2K likely contributes to neuronal function by regulating the synthesis of microtubule-related proteins. Phosphorylation of elongation factor 2, EF2, results in slower elongation which then result in the increased synthesis of specific proteins. Expression levels of eEF2K targets with unaltered, enhanced, and reduced eEF2K enzyme activity, overview. Synthesis of MAP1B, ARC, and CAMKIIa is sensitive to eEF2K inhibition
physiological function
elongation factor-2 kinase (eEF2K), a protein kinase that suppresses protein synthesis during elongation phase, is a positive regulator of apoptosis both in vivo and in vitro. eEF2K is required for G2/M arrest induced by radiation to prevent mitotic catastrophe in a p53-independent manner in epithelial cells. eEF2K also provides a protective strategy to maintain genomic integrity by arresting cell cycle in response to stress. 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. The dynamics of eEF2K activity in DNA damage response is distinct in different cell types and are related to cell proliferating status. eEF2K suppresses intestinal mitotic cell death in response to gamma-irradiation
physiological function
transcription elongation is controlled by phosphorylation of eukaryotic elongation factor 2 (eEF2), which inhibits its activity and is catalyzed by eEF2 kinase (eEF2K), a calcium/calmodulin-dependent alpha-kinase. eEF2K activity is regulated through several signaling pathways linked, e.g., to nutrient availability. Hypoxia causes the activation of eEF2K and induces eEF2 phosphorylation. eEF2K is subject to hydroxylation on proline 96. Proline hydroxylation is catalyzed by proline hydroxylases, oxygen-dependent enzymes which are inactivated during hypoxia. Hypoxia-induced eEF2 phosphorylation requires eEF2K and is not catalyzed by AMPK, it does also not require signaling via AMPK or mTORC1. Pharmacological inhibition of proline hydroxylases, e.g. by DMOG treatment, also stimulates eEF2 phosphorylation. Pro96 lies in a universally conserved linker between the calmodulin-binding and catalytic domains of eEF2K. Its hydroxylation partially impairs the binding of calmodulin to eEF2K and markedly limits the calmodulin-stimulated activity of eEF2K. Neuronal cells depend on oxygen, and eEF2K helps to protect them from hypoxia. eEF2K is cytoprotective during hypoxia and other conditions of nutrient insufficiency, it aids the survival of neuronal cells during hypoxia and has a key role in helping cells withstand nutrient deficiency
physiological function
cardiac hypertrophy may be regulated at least partly via enzyme-eukaryotic elongation factor 2 signaling pathway
malfunction
-
in vivo studies with Gcn2 knockout mice show increased susceptibility to both acute or chronic liver damage induced by CCl4, as shown by higher alanine aminotransferase and aspartate aminotransferase activities, increased necrosis and higher inflammatory infiltrates compared with wild-type mice. Chronic CCl4 treatment increases deposition of interstitial collagen type I. Col1a1 and col1a2 mRNA levels also increase in CCl4-treated Gcn2-/- mice compared with wild-type mice
physiological function
-
the eIF2 kinase GCN2 is essential for the murine immune system to adapt to amino acid deprivation by asparaginase
physiological function
-
the enzyme is a key regulator of the fibrogenic response to liver injury
physiological function
-
the enzyme is implicated in induction of apoptosis and endoplasmic reticulum stress-responsive genes by sodium salicylate
physiological function
in response to amino acid starvation, GCN2 phosphorylation of eukaryotic initiation factor 2 leads to repression of general translation and initiation of gene reprogramming that facilitates adaptation to nutrient stress
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). EF2K_MOUSE
724
0
81739
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
side-chain modification
eEF2K is subject to hydroxylation on proline 98 catalyzed by proline hydroxylases
phosphoprotein
phosphoprotein
AMPK activates eEF2K via phosphorylation. Inhibition of proline hydroxylases, e.g. by DMOG, induces the phosphorylation of eEF2 independently of altered mTORC1 or AMPK signaling
phosphoprotein
the enzyme is phosphorylated by diverse kinases with stimulating or suppressing effect, the enzyme is regulated by its phosphorylation status, overview
phosphoprotein
-
phosphorylation by p70-S6 kinase inhibits EF2K, Ca2+ decreases the phosphorylation of the enzyme
phosphoprotein
-
phosphorylation of eEF2K can either inhibit or enhance the activity of its downstream substrate, depending on the site of phosphorylation and the type of stimul, lopinavir increases the phosphorylation of eEF2 kinase on Ser366 reducing its activity, LPV affects eEF2 activity via an AMPK-eEF2K dependent pathway, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 5.5) and 21-28% (w/v) polyethylene glycol 2000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of gene eEF-2K deletion mutants, phenotype, overview
additional information
generation of eEF2K knockout mice and eEF2K knock-in mice, phenotype, overview
additional information
-
GCN2-deficient mice fed a leucine-deprived diet, develop liver steatosis, genes related to triglyceride synthesis and expression of SREBP-1c and PPARg are not repressed. Beta-oxidation genes and fatty-acid transport genes are upregulated, mutant exhibits reduced lipid mobilization
additional information
-
construction of Gcn2 knockout mice and effects on enzyme activity and leucine metabolism, phenotype, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and mutant eEF2K enzymes from Escherichia coli strain Rosetta(DE3)pLysS
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant overexpression of FLAG-tagged enzyme from pcDNA3.1 vector in HEK-293 cells, recombinant expression of GST-tagged wild-type and mutant eEF2K enzymes in Escherichia coli strain Rosetta(DE3)pLysS
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of the mRNA for EEF2K is probably regulated in multiple ways, e.g. downstream of AMPK, and in some settings by mTORC1 signaling and HIF1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the enzyme is a valuable target in treating epilepsy, depression and major neurodegenerative diseases
additional information
additional information
-
eEF2 kinase does not play a role in regulating elongation factor 2
additional information
-
novel function of GCN2, regulates lipid metabolism during leucine deprivation in addition to regulating amino acid metabolism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryazanov, A.G.; Ward, M.D.; Mendola, C.E.; Pavur, K.S.; Dorovkov, M.V.; Wiedmann, M.; Erdjument-Bromage, H.; Tempst, P.; Parmer, T.G.; Prostko, C.R.; Germino, F.J.; Hait, W.N.
Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase
Proc. Natl. Acad. Sci. USA
94
4884-4889
1997
Caenorhabditis elegans (O01991), Caenorhabditis elegans, Homo sapiens (O00418), Homo sapiens, Mus musculus (O08796), Mus musculus, Rattus norvegicus (P70531)
Guo, F.; Cavener, D.R.
The GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of an essential amino acid
Cell Metab.
5
103-114
2007
Mus musculus, Mus musculus C57/BL6J
Hong-Brown, L.Q.; Brown, C.R.; Huber, D.S.; Lang, C.H.
Alcohol regulates eukaryotic elongation factor 2 phosphorylation via an AMP-activated protein kinase-dependent mechanism in C2C12 skeletal myocytes
J. Biol. Chem.
282
3702-3712
2007
Mus musculus
Sataranatarajan, K.; Mariappan, M.M.; Lee, M.J.; Feliers, D.; Choudhury, G.G.; Barnes, J.L.; Kasinath, B.S.
Regulation of elongation phase of mRNA translation in diabetic nephropathy: amelioration by rapamycin
Am. J. Pathol.
171
1733-1742
2007
Mus musculus
Crawley, S.W.; Cote, G.P.
Determinants for substrate phosphorylation by Dictyostelium myosin II heavy chain kinases A and B and eukaryotic elongation factor-2 kinase
Biochim. Biophys. Acta
1784
908-915
2008
Mus musculus
Boyce, M.; Py, B.F.; Ryazanov, A.G.; Minden, J.S.; Long, K.; Ma, D.; Yuan, J.
A pharmacoproteomic approach implicates eukaryotic elongation factor 2 kinase in ER stress-induced cell death
Cell Death Differ.
15
589-599
2008
Mus musculus (O08796)
Clark, K.; Middelbeek, J.; Dorovkov, M.V.; Figdor, C.G.; Ryazanov, A.G.; Lasonder, E.; van Leeuwen, F.N.
The alpha-kinases TRPM6 and TRPM7, but not eEF-2 kinase, phosphorylate the assembly domain of myosin IIA, IIB and IIC
FEBS Lett.
582
2993-2997
2008
Mus musculus
Hong-Brown, L.Q.; Brown, C.R.; Huber, D.S.; Lang, C.H.
Lopinavir impairs protein synthesis and induces eEF2 phosphorylation via the activation of AMP-activated protein kinase
J. Cell. Biochem.
105
814-823
2008
Mus musculus
Bunpo, P.; Cundiff, J.K.; Reinert, R.B.; Wek, R.C.; Aldrich, C.J.; Anthony, T.G.
The eIF2 kinase GCN2 is essential for the murine immune system to adapt to amino acid deprivation by asparaginase
J. Nutr.
140
2020-2027
2010
Mus musculus
Gentz, S.H.; Bertollo, C.M.; Souza-Fagundes, E.M.; da Silva, A.M.
Implication of eIF2alpha kinase GCN2 in induction of apoptosis and endoplasmic reticulum stress-responsive genes by sodium salicylate
J. Pharm. Pharmacol.
65
430-440
2013
Mus musculus
Arriazu, E.; Ruiz de Galarreta, M.; Lopez-Zabalza, M.J.; Leung, T.M.; Nieto, N.; Iraburu, M.J.
GCN2 kinase is a key regulator of fibrogenesis and acute and chronic liver injury induced by carbon tetrachloride in mice
Lab. Invest.
93
303-310
2013
Homo sapiens, Mus musculus
He, H.; Singh, I.; Wek, S.; Dey, S.; Baird, T.; Wek, R.; Georgiadis, M.
Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals
J. Biol. Chem.
289
15023-15034
2014
Saccharomyces cerevisiae (P15442), Mus musculus (Q9QZ05)
Kenney, J.W.; Moore, C.E.; Wang, X.; Proud, C.G.
Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles
Adv. Biol. Regul.
55
15-27
2014
Homo sapiens, Mus musculus (O08796)
Liao, Y.; Chu, H.P.; Hu, Z.; Merkin, J.J.; Chen, J.; Liu, Z.; Degenhardt, K.; White, E.; Ryazanov, A.G.
Paradoxical roles of elongation factor-2 kinase in stem cell survival
J. Biol. Chem.
291
19545-19557
2016
Mus musculus (O08796)
Kenney, J.W.; Genheden, M.; Moon, K.M.; Wang, X.; Foster, L.J.; Proud, C.G.
Eukaryotic elongation factor 2 kinase regulates thesynthesis of microtubule-related proteins in neurons
J. Neurochem.
136
276-284
2016
Mus musculus (O08796), Mus musculus, Mus musculus C57/BL6J (O08796)
Moore, C.E.; Mikolajek, H.; Regufe da Mota, S.; Wang, X.; Kenney, J.W.; Werner, J.M.; Proud, C.G.
Elongation factor 2 kinase is regulated by proline hydroxylation and protects cells during hypoxia
Mol. Cell. Biol.
35
1788-1804
2015
Homo sapiens (O00418), Mus musculus (O08796)
Kameshima, S.; Okada, M.; Ikeda, S.; Watanabe, Y.; Yamawaki, H.
Coordination of changes in expression and phosphorylation of eukaryotic elongation factor 2 (eEF2) and eEF2 kinase in hypertrophied cardiomyocytes
Biochem. Biophys. Rep.
7
218-224
2016
Mus musculus (O08796), Rattus norvegicus (P70531)
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