Editing of the polyubiquitin architecture on the collided ribosome maintains persistent RQC activity

2025 · doi:10.1101/2025.04.23.650188
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The paper investigates how ribosome-associated quality control maintains and recycles ubiquitin polyubiquitin chains on colliding stalled ribosomes, focusing on K63-linked polyubiquitination of uS10 and how it is edited over time. Using yeast RQC-related mechanisms, the authors identify two deubiquitinating enzymes, Ubp2 and Ubp3, with distinct roles: Ubp2 removes the K63-linked polyubiquitin chain from uS10 on the free 40S subunit for recycling, while Ubp3 cleaves K48-linked di-ubiquitin and K48/K63-mixed linkage chains from uS10 on translating ribosomes, sustaining RQC activity. A key finding is that K48-containing ubiquitin chains on uS10 of colliding ribosomes act as a negative signal that suppresses RQT-mediated ribosome dissociation. The study is limited to the defined RQC ubiquitin “code” and enzyme functions described in their experimental system. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

In Ribosome-associated Quality Control (RQC), K63-linked polyubiquitination of uS10 on the stalled ribosome is crucial for recruiting the RQC-trigger (RQT) complex. However, the mechanisms governing the maintenance and recycling of polyubiquitin architecture on colliding ribosomes remain unclear. Here we demonstrate that two deubiquitinating enzymes (DUBs), Ubp2 and Ubp3, play key roles in editing and recycling polyubiquitin chains on uS10, thereby contributing to the promotion of RQC activity. Specifically, Ubp2 eliminates the K63-linked polyubiquitin chain from uS10 on the free 40S subunit for recycling, while Ubp3 predominantly cleaves the K48-linked di-ubiquitin and the K48/K63-mixed-linkage poly-ubiquitin chain from uS10 on the translating ribosomes. Notably, we further demonstrate that the ubiquitin chains containing K48-linkage of the uS10 on the colliding ribosome act as a negative signal for the RQT-mediated ribosome dissociation process. Collectively, our findings clarify the ubiquitin code in RQC and define the positive functions of these two DUBs in maintaining the persistent RQC activity.
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Abstract In Ribosome-associated Quality Control (RQC), K63-linked polyubiquitination of uS10 on the stalled ribosome is crucial for recruiting the RQC-trigger (RQT) complex. However, the mechanisms governing the maintenance and recycling of polyubiquitin architecture on colliding ribosomes remain unclear. Here we demonstrate that two deubiquitinating enzymes (DUBs), Ubp2 and Ubp3, play key roles in editing and recycling polyubiquitin chains on uS10, thereby contributing to the promotion of RQC activity. Specifically, Ubp2 eliminates the K63-linked polyubiquitin chain from uS10 on the free 40S subunit for recycling, while Ubp3 predominantly cleaves the K48-linked di-ubiquitin and the K48/K63-mixed-linkage poly-ubiquitin chain from uS10 on the translating ribosomes. Notably, we further demonstrate that the ubiquitin chains containing K48-linkage of the uS10 on the colliding ribosome act as a negative signal for the RQT-mediated ribosome dissociation process. Collectively, our findings clarify the ubiquitin code in RQC and define the positive functions of these two DUBs in maintaining the persistent RQC activity.

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