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Novel regulation of the eEF2K/eEF2 pathway: prospects of ‘PQBP1 promotes translational elongation and regulates hippocampal mGluR-LTD by suppressing eEF2 phosphorylation’
Yuqian Shen1,2 , Junhai Han1,2,* , Zi Chao Zhang1,2,*
1School of Life Science and Technology, Key Laboratory of Developmental Genes and Human Disease, Southeast University, Nanjing 210096, China
2Co-innovation Center of Neuroregeneration, Nantong University, Nantong 226001, China
*Correspondence to:Junhai Han , Zi Chao Zhang ,
J Mol Cell Biol, Volume 13, Issue 5, May 2021, 392-394,

Protein synthesis involves initiation, elongation, and termination. A number of studies show that translation elongation is highly regulated and is the most energy-intensive process, which controls the efficiency and accuracy of protein synthesis. In the elongation process, eukaryotic elongation factor 2 (eEF2) binds to the ribosome to induce its conformation change and promotes the translocation of the tRNAs by hydrolyzing guanosine triphosphate, which then allows the next AA-tRNA to enter the A site for translation elongation. The activity of eEF2 is negatively regulated by its kinase eEF2K that phosphorylates eEF2 at threonine-56 (Thr56). Dysregulation of elongation is the core of the pathogenesis of tumorigenesis and neurodegeneration. Thus, eEF2/eEF2K as a potential therapeutic target has attracted more and more attention (Knight et al., 2020). In a recently published work, we identified that the intellectual disability related protein, polyglutamine-binding protein 1 (PQBP1), is a novel regulator that binds directly with eEF2 and affects its phosphorylation (Figure 1; Shen et al., 2021).