Eef2k Antibodies

Eukaryotic elongation factor 2 kinase (Eef2k)

Threonine kinase that modulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single website, renders it unable to bind ribosomes and thus inactive.

Subsequently, the rate of protein synthesis is decreased. .

Gene Information

Mouse
Gene Name:	Eef2k
Uniprot:	O08796
Entrez:	13631

Family

Belongs to:
protein kinase superfamily

Alternative Names

Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase; calcium/calmodulin-dependent eukaryotic elongation factor-2 kinase; EC 2.7.11; EC 2.7.11.20; eEF-2 kinase; eEF-2Kcalmodulin-dependent protein kinase III; elongation factor-2 kinase; eukaroytic elongation factor 2 kinase; eukaryotic elongation factor 2 kinase; eukaryotic elongation factor-2 kinase; HSU93850; MGC45041

Molecular Weight

Mass (kDA):
81.739 kDA

Genomic Context

Mouse
Location:	7|7 F2
Sequence:	7;

Tissue Specificity

Ubiquitously expressed. Particularly abundant in skeletal muscle and heart.

Diseases

• Malignant Neoplasms
• Neoplasms
• Glioma
• Hypertrophy
• Glioblastoma
• Malignant Paraganglionic Neoplasm
• Malignant Neoplasm Of Breast
• Hypoxia
• Physiological Stress
• Cell Transformation, Neoplastic
• Hyperplasia
• Sclerosis
• Cardiac Hypertrophy

• Carcinoma
• Ischemia
• Atrophy
• Depressive Disorder
• Muscular Atrophy
• Brain Neoplasms
• Hiv Infections

Pathways

• Translation
• Cell Proliferation
• Cell Cycle
• Autophagy
• Protein Phosphorylation
• Cell Death
• Regulation Of Translation
• Rna Interference
• Energy Homeostasis
• Cell Growth
• Response To Nutrient
• Oncogenesis
• Mitosis

• Translational Elongation
• Pathogenesis
• Regulation Of Protein Phosphorylation
• Transport
• Mitochondrial Outer Membrane Permeabilization
• Muscle Contraction
• Regulation Of Autophagy

PTMs

• Phosphorylation
• Dephosphorylation

• Cleavage
• Ribosylation

• Ubiquitination

Research Areas

• Cancer

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/Eef2k

Best Uses Of The EEF2K Marker

Boster Bio validated the EEF2K mark by comparing the binding patterns to known positive and non-positive samples. In addition to its potential applications in research, this marker is also useful for identification of ebola virus. It has demonstrated improved viability in cell lines, reduced AS toxicity, as well as increased viability in cultured cells. Read the article below to learn more about EEF2K.

eEF2K kd reduces AS toxicity

AS toxicity is thought to be a major cause of neurodegeneration in patients with Parkinson's disease. AS toxicity is a major factor in neurodegeneration. It can be caused by overexpression of the protein, which promotes aggregation and increases oxidative strain, and impairs cells' survival. AS mutation A53T leads to neurodegeneration, pathology and accelerated aggregation.

Parkinson disease is the leading cause. Pathologic accumulations (AS) of alphasynuclein may trigger neurotoxic mechanism. PD has been linked to eEF2K, a protein that plays an important role in synaptic plasticity as well as dendritic mRNA transcription. Postmortem PD brains showed an increase in phosphorylation on serine residue 56 of eEF2K.

In mice undergoing PD, phospho-eEF2 and phospho-AS are phosphorylated at Thr56 and Ser129, respectively. Pre-formed fibrillarAS improves motor phenotypes, and survival. AS toxicities can have other effects. It can cause disruptions in mitochondrial respiration and mass. These results are encouraging for future research into the neurodegenerative effects that AS can have on the brain.

72 hours after transfection, cell viability was reduced by the overexpression of ASynWT and –A53T. This was measured using flow cytometry analysis of PI staining. AS toxicity was also reduced by eEF2K. Its use as an AS therapy may help reduce the incidences of neurodegeneration. The results are promising, even though we don't yet have conclusive evidence.

eEF2K kd enhances mitochondrial respiration. eEF2K kd cells show an increase in cellular metabolism. The mtDNA content and mitochondrial mass did not differ between eEF2K Kd cells and control cells. Despite the same mitochondrial mass, the mitochondrial functions increased.

eEF2K kd is a possible method to identify ebolavirus.

The eEF2K kd genome is a key component of the antigenome Ebola virus. There are more than 30 known viruses which can cause hemorhagic febrile illness. Only one, the Ebola virus, is capable of causing the fatal disease. The virus is classified into five species: Sudan, Zaire, Reston, and Bundibugyo. The Zaire strain caused Ebola's largest epidemic in history.

ELISA or RT/QPCR are quick blood tests to confirm EBOV infection. The detection of EBOV can be done using paper-based immunoassays, or nanotechnology based colorimetrics. However, these methods can only be used in laboratory settings. Ebola infection can be confirmed using state-of the-art diagnostics in as little as 6 hours to three days. Ebola diagnostics will be made more efficient and sensitive by the development of cost-effective sensors.

Antigen capture ELISA and RNA detect by RTPCR are two types of rapid blood tests that can be used to diagnose EBOV. The ELISA testing procedure is time-consuming for health care workers. It requires multiple washes of ELISA plates. The RTPCR test is not available in the field. Ebola rapid diagnostics take at least three days. This delays the therapeutic approach.

Ebola virus symptoms can appear in early stages of the disease. Sometimes, even if a patient does not have symptoms, they can be tested for Ebola virus disease after three days. Ebola fever is a serious illness that pregnant women should be tested. If you have any of these symptoms or you know someone who has, it's important to get medical attention right away.

The immunofluorescent method is another way to detect EBOV. This method uses HeLa cells to express a Baculovirus recombinant (NP) that carries Ebola. This antibody reacts with the corresponding NP region. The antibody should be used in a BSL-4 facility to detect ebola virus antibodies.

eEF2K kd has been suggested as a potential drug target in cancer therapy. This protein can also be used as a treatment for depressive disorders. To illustrate the mechanism of inhibition, a steady-state kinetic model was created using a peptide substrate. This enzyme exhibits an ordered sequential mechanism in which it inhibits substrate eEF2K by a competitive mechanism. Several small molecules have been created to inhibit eEF2K because the enzyme inhibits its substrate by a competitive mechanism.

eEF2KK kd improves viability within cultures

The overall cellular level of ATP was significantly affected by the loss of eEF2K or 4EBP1. The loss of eEF2K/4EBP1 could lead to a reduction in cellular ATP due to excess protein translation. These results suggest that eEF2K Kd may be cytoprotective against cancer cells. Further studies are needed to determine if eEF2K kd is cytoprotective for cancer cells.

Transfection of eEF2K kd into lung cancer cells has been shown to significantly inhibit cell invasion in vitro. Moreover eEF2K knockdown significantly reduced matrigel invading cells compared to control. Furthermore, knockdown of eEF2K reduces the proliferation and invasion of TNBC cells, recapitulating the effect of miR603 in this context.

To determine whether eEF2K kd increase cell viability in cultured tissues, A549 cells underwent 16 hours of incubation with 3 mM Jan-384 and 10 mg 2-deoxyglucose (2DG). Cells were then harvested and lysed to examine protein expression using the indicated antibodies. The P-eEF2 was then normalized with eEF2 and the average + SEM of this experiment was calculated.

To test the hypothesis that eEF2K depletion improves cell viability in cultured cells, scientists tested eEF2K inhibitors in mouse models. JAN-384 was found highly active and JAN-452 inactive. JAN-849, on the other hand, was inactive at 30 mM against eEF2K. The compound JAN-849 was well tested against eEF2K and CLK2, GSK3a and GSK3b, as well as CDK7.

As the ability of cancer cells to survive glucose starvation is impaired by inhibition of eEF2K, activation of eEF2K rescued the cellular viability. This suggests that eEF2K is involved in the survival of cancer cells including gliomas. Moreover, eEF2K loss can reduce the energy requirements for protein synthesis and thus decrease metabolic fuel needs.

Knockdown eEF2K through RNAi significantly raises the levels of CDK1 & COL1A1. In addition, eEF2K depletion decreases the levels of CDK1 and 4EBP1 in all cell lines, and the cells with both KO and 4EBP1 knockdown are more viable than those without eEF2K-KO.

Inhibiting eEF2K causes inhibition of protein synthesis which is vital for cell survival. It promotes autophagy, which is crucial for survival in nutrient-starved environments. It is not clear how eEF2K regulates autophagy. This protein is essential in many aspects.

Knockdown of eEF2K decreased the expression of p-EF2K, Src, Akt, Fak, and MYP19. MiR-603 also inhibited eEF2K expression in MDA-MB-231 cells and BT-20 cells. These data suggest the possibility that miR-603 regulates eEF2K expression by TNBC-cells.