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Last update 08 May 2025

EEF2

Last update 08 May 2025

Basic Info

Synonyms

EEF-2, EEF2, EF-2

+ [5]

Introduction

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721).

Drugs associated with EEF2

FR290581

Target

EEF2

Mechanism

EEF2 inhibitors

Active Org.-

Originator Org.

Astellas Pharma, Inc.

Active Indication-

Inactive Indication

Mycoses

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

LV-1053

Target

EEF2

Mechanism

EEF2 inhibitors

Active Org.-

Originator Org.

Longevica Pharmaceuticals, Inc.

Active Indication-

Inactive Indication

Heart Injuries [+1]

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

NSC-745343

Target

EEF2 x HKs

Mechanism

EEF2 gene inhibitors [+1]

Active Org.-

Originator Org.

Mayo Clinic

Active Indication-

Inactive Indication

Neoplasms

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with EEF2

100 Translational Medicine associated with EEF2

0 Patents (Medical) associated with EEF2

2,160

Literatures (Medical) associated with EEF2

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 Jul 2025·The International Journal of Biochemistry & Cell Biology

Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome

Article

Author: Steele, Jacob H ; Stepanov, Victor G ; Lin, Ran ; Gavriliuc, Miriam N ; Johnson, Jordan L ; Wang, Yuhong

While elongation factor G (EF-G) is crucial for ribosome translocation, the role of its GTP hydrolysis remains ambiguous. EF-G's indispensability is further exemplified by the phosphorylation of human eukaryotic elongation factor 2 (eEF2) at Thr56, which inhibits protein synthesis globally, but its exact mechanism is not clear. In this study, we developed a multi-channel single-molecule FRET (smFRET) microscopy methodology to examine the conformational changes of E. coli EF-G induced by mutations that closely aligned with eEF2's Thr56 residue. We utilized Alexa 488/594 double-labeled EF-G to catalyze the translocation of fMet-Phe-tRNA^Phe-Cy3 inside Cy5-L27 labeled ribosomes, allowing us to probe both processes within the same complex. Our findings indicate that in the presence of either GTP or GDPCP, wild-type EF-G undergoes a conformational extension upon binding to the ribosome to promote normal translocation. On the other hand, the T48E and T48V mutations did not affect GTP/GDP binding or GTP hydrolysis, but impeded Poly(Phe) synthesis and caused EF-G to adopt a unique compact conformation, which was not observed when the mutants interact solely with the SRL. This study provides new insights into EF-G's adaptability and sheds light on the modification mechanism of human eEF2.

01 Jun 2025·Comparative Biochemistry and Physiology Part D: Genomics and Proteomics

High-throughput screening of thermal tolerant candidate genes in the ivory shell (Babylonia areolata) based on the yeast strain INVSc1

Article

Author: Zheng, Xing ; Fu, Deng ; Ke, Caihuan ; Gu, Zhifeng ; Zhang, Meng ; Vasquez, Hebert Ely ; Wu, Yingyin ; Cai, Haonan ; Wang, Aimin ; Zou, Yu ; Liu, Chunsheng ; Qin, Jie ; Zhu, Yanyun ; Yu, Feng

Global climate warming and frequent heatwaves present significant threats to the growth and survival of marine organisms. The ivory shell, Babylonia areolata, plays a crucial role in marine aquaculture as a widely distributed mollusk in tropical and subtropical seas. However, limited research has been conducted on its molecular mechanisms in response to heat stress. This study aims to explore thermal-tolerant related genes and regulatory pathways by constructing a cDNA library under heat stress and using a yeast-based high-throughput screening method. Following exposure of three populations to acute heat stress, a heat stress cDNA library was constructed with a capacity of 1.104 × 10⁸, containing 2.208 × 10⁸ clones. Subsequently, the library was transformed into yeast INVSc1 and underwent high-temperature screening at 39 °C. All positive clones were then subjected to next-generation sequencing (NGS) for rapid identification of 1148 candidate genes associated with thermal tolerance. Enrichment analysis revealed that these genes were significantly enriched in seven KEGG pathways, including Protein processing in endoplasmic reticulum, Ribosome and Ubiquitin mediated proteolysis. Additionally, through first-generation sequencing of 96 randomly selected positive clones at 39 °C, we identified 51 unique sequences associated with heat stress which included previously reported genes like EEF2, HSPB1, UBC and HSPA4. Subsequent yeast heat tolerance experiments further validated the essential role played by these 51 genes in response to thermal stress conditions. Finally, RNA-seq data provided evidence for upregulated expression levels of these genes during exposure to elevated temperatures. This study successfully constructed the first cDNA library for B. areolata under heat stress conditions, identified key pathways and candidate genes associated with thermal tolerance, and demonstrated the applicability of yeast high-throughput screening methods in investigating stress resistance traits in invertebrates. These findings contribute to a deeper understanding of the strategies employed by B. areolata to respond to heat stress, and provide technical support for studying the molecular mechanisms underlying abiotic stress responses in aquatic organisms.

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EEF2

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