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The dynamic tuning of protein synthesis in response to environmental cues is a fundamental hallmark of life, yet the mechanisms governing post-termination ribosome recycling remain poorly understood. While translation is traditionally categorized into initiation, elongation, and termination, competent subunits must be efficiently recycled following peptide release to sustain subsequent rounds of protein synthesis. We investigate eukaryotic initiation factor 6 (eIF6), an anti-association factor that binds the 60S subunit, and identified its phosphorylation as a critical requirement for efficient ribosome recycling following termination. Phospho-eIF6 levels are stimulated by growth signals and suppressed during viral infection; its loss sharply reduces translation and triggers a distinct quiescent state termed RESt (Respiratory Energetic Stop), independent of the integrated stress response. Furthermore, loss of phospho-eIF6 completely blocks tumorigenesis in an ALK-driven T-cell lymphoma model while inducing senescence and inflammatory signaling, establishing eIF6 as a translational checkpoint that coordinates ribosome recycling, mitochondrial dynamics, and tumor suppression
