USP9X promotes the degradation of trapped translation factors on collided ribosomes.

USP9X is essential for degrading ubiquitinated eRF1 on collided ribosomes by trimming K6-linked ubiquitin chains in quality control pathways.

• Why it matters: Efficient removal of stalled translation factors is crucial for maintaining translation fidelity and preventing cellular stress, but the specific role of USP9X in this process was unclear.
• What they did: The study used molecular and cellular approaches to show that USP9X regulates the degradation of ubiquitinated eRF1, with its absence leading to accumulation of K6-linked ubiquitin chains on eRF1.
• The result: Impaired USP9X activity prevents eRF1 degradation and translation shutdown, indicating that USP9X facilitates late-stage substrate processing and influences the integrated stress response.