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Last update 08 May 2025

EEF2K

Last update 08 May 2025

Basic Info

Synonyms

Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase, CaMKIII, eEF-2 kinase

+ [3]

Introduction

Threonine kinase that regulates 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 site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.

Drugs associated with EEF2K

EEF2K inhibitors(Central South University)

Target

EEF2K

Mechanism

EEF2K inhibitors

Active Org.

Central South University

Originator Org.

Central South University

Active Indication

Triple Negative Breast Cancer

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

A-484954

Target

EEF2K

Mechanism

EEF2K inhibitors

Active Org.

Abbott Laboratories

Originator Org.

Abbott Laboratories

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

CN118994100

Patent Mining

Target

EEF2K

Mechanism

EEF2K inhibitors

Active Org.

Soochow University [+1]

Originator Org.

Soochow University [+1]

Active Indication

Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with EEF2K

100 Translational Medicine associated with EEF2K

0 Patents (Medical) associated with EEF2K

384

Literatures (Medical) associated with EEF2K

01 Dec 2025·Molecular Biology Reports

Comparing the malignant properties of parental and a knock-in version of HCT116 cell line expressing the CDK2-mutant of eukaryotic elongation factor 2 (eEF2)

Article

Author: Yüksel, B ; Deniz, A Aslı Hızlı ; Şahin, F ; Türkel, N

BACKGROUNDModulation of protein synthesis according to the physiological cues is maintained through tight control of Eukaryotic Elongation Factor 2 (eEF2), whose unique translocase activity is essential for cell viability. Phosphorylation of eEF2 at its Thr56 residue inactivates this function in translation. In our previous study we reported a novel mode of post-translational modification that promotes higher efficiency in T56 phosphorylation. Cyclin A/CDK2-mediated phosphorylation of eEF2 at the S595 residue is required for more potent phosphorylation at the Thr56, suggesting CDK2 takes a role in robust suppression of protein synthesis.METHODS AND RESULTSIn the current study, we analyzed the cell cycle, proliferation, cell death, migration, colony formation, autophagy, and response to Cisplatin properties of the point-mutant variant of HCT116 cells that express the CDK2 mutant (S595A-eEF2) of eEF2. The knocked in S595A mutation resulted in decreased levels of T56 phosphorylation of eEF2, which appears to have similar biological consequences to other experimental manipulations such as silencing the activity of the kinase for the Thr56 residue, eEF2 Kinase (eEF2K).CONCLUSIONOur findings indicate that interfering with the inhibition of eEF2 results in elevated protein synthesis in HCT116 cells and is associated with the progression of malignancy in the colorectal cancer cell line, where eEF2K activity could provide a tumor suppressive role.

01 Jun 2025·JOR SPINE

Molecular Subtypes and Immune Microenvironment Characterization of the Annulus Fibrosus in Intervertebral Disc Degeneration: Insights From Translation Factor‐Related Gene Analysis

Article

Author: Zhao, Xiaokun ; He, Dingwen ; Cuan, Xuhui ; Cheng, Xigao ; Zheng, Sikuan ; Wu, Hui

ABSTRACTObjectiveThis study aims to examine the role of translation factors (TF) in intervertebral disc degeneration (IVDD) and to evaluate their clinical relevance through unsupervised clustering methods.MethodsGene expression data were retrieved from the GEO database, and the expression levels of translation factor‐related genes (TFGs) were extracted for analysis.ResultsTwo distinct molecular clusters were identified based on the differential expression of nine significantly altered TFGs. Immune infiltration was notably higher in Cluster C2 compared to Cluster C1. Subsequently, two gene clusters were identified based on the differentially expressed genes between the clusters. A Sankey diagram illustrated a high degree of consistency between the molecular clusters and the gene clusters. Additionally, four machine learning models were developed and evaluated, with the SVM model being utilized to construct a nomogram for predicting the incidence of IVDD. Validation using external datasets and clinical samples confirmed the low expression of EEF2K, which was further analyzed in a pan‐cancer context.ConclusionThe identification and comprehensive assessment of the two molecular clusters offer significant insights for the classification and treatment of individuals with IVDD.

01 Apr 2025·Advanced Science

Identification of a Novel Substrate for eEF2K and the AURKA‐SOX8 as the Related Pathway in TNBC

Article

Author: Ye, Na ; Jiang, Shilong ; Gong, Rong ; Yang, Jinming ; Cao, Shijun ; Shan, Tianjiao ; He, Linhao ; Tian, Sheng ; Yi, Wenjun ; Zhu, Rongfeng ; Chen, Zonglin ; Cheng, Yan ; Wan, Xiaoya ; Zhong, Changxin ; Zhao, Xiaobao ; Li, Yizhi

AbstractEukaryotic elongation factor 2 kinase (eEF2K) has been considered as a putative target for cancer therapy; however, the underlying mechanisms of eEF2K in triple‐negative breast cancer (TNBC) progression remain to be fully elucidated. In this study, it is shown that eEF2K is highly expressed in TNBC and is associated with poor prognosis. In vitro, in vivo, and patient‐derived organoid experiments demonstrate that knockdown of eEF2K significantly impedes progression of TNBC. Proteomic analysis and confirmation experiments reveal that eEF2K positively regulates the mRNA and protein expressions of sex‐determining region Y‐box 8 (SOX8). Mechanistically, eEF2K binds to and phosphorylates aurora kinase A (AURKA) at S391, a newly identified phosphorylation site critical for maintaining AURKA protein stability and kinase activity. Moreover, the compound C1, a molecular glue to degrade eEF2K, is optimized by designing and synthesizing its derivatives using reasonable structure‐based optimization approach. The new compound C4 shows better ability to degrade eEF2K and stronger anti‐cancer activity than C1. These findings not only uncover the pivotal role of the eEF2K/AURKA/SOX8 axis in TNBC progression, but also provide a promising lead compound for developing novel drug for treatment of TNBC.

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