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Significance Following infection and inflammation, activation of the transcription factor NF-κB and stimulation of mRNA translation initiation remodel cellular gene expression. In contrast, how translation elongation factor 2, which performs the translocation step in protein synthesis, responds is not understood. We show that eEF2 Thr56 phosphorylation, which slows elongation, and eEF2 kinase (eEF2K) abundance are reduced by multiple NF-κB–activating stimuli. Significantly, NF-κB activation repressed eEF2K transcription to stimulate eEF2 by preventing eEF2 phosphorylation. In addition, eEF2K abundance regulates protein synthesis upon eEF2 inactivation by a bacterial toxin. This demonstrates how eEF2 is integrated into NF-κB innate immune response networks and reveals an unexpected mechanism whereby regulated nuclear transcription impacts translation elongation.

Repression of eEF2K transcription by NF-κB tunes translation elongation to inflammation and dsDNA-sensing