Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways
Open accessAbstract
Ribosome stalling triggers quality control pathways targeting the mRNA (NGD: no-go decay) and the nascent polypeptide (RQC: ribosome-associated quality control). RQC requires Hel2-dependent uS10 ubiquitination and the RQT complex in yeast. Here, we report that Hel2-dependent uS10 ubiquitination and Slh1/Rqt2 are crucial for RQC and NGD induction within a di-ribosome (disome) unit, which consists of the leading stalled ribosome and the following colliding ribosome. Hel2 preferentially ubiquitinated a disome over a monosome on a quality control inducing reporter mRNA in an in vitro translation reaction. Cryo-EM analysis of the disome unit revealed a distinct structural arrangement suitable for recognition and modification by Hel2. The absence of the RQT complex or uS10 ubiquitination resulted in the elimination of NGD within the disome unit. Instead, we observed Hel2-mediated cleavages upstream of the disome, governed by initial Not4-mediated monoubiquitination of eS7 and followed by Hel2-mediated K63-linked polyubiquitination. We propose that Hel2-mediated ribosome ubiquitination is required both for canonical NGD (NGD RQC+) and RQC coupled to the disome and that RQC-uncoupled NGD outside the disome (NGD RQC-) can occur in a Not4-dependent manner.
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If anabolic signaling drives high rates of translation without sufficient recovery or quality control, resulting translational errors may activate stress responses that impair protein synthesis efficiency.
“If anabolic signaling drives high rates of translation without sufficient recovery or quality control, the resulting increase in translational errors may activate stress responses that ultimately impair protein synthesis efficiency [208,209,210].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [210]
The Introduction (page unavailable) describes stalled or collided ribosomes initiating quality-control pathways, supporting the general link between translation problems and a cellular response. It does not say that anabolic signaling or insufficient recovery increases translational errors, or that the response impairs protein-synthesis efficiency. (LLM, conf=0.82)
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References 51 · Cited by 315
- Authors
- Ikeuchi, K., Tesina, P., Matsuo, Y., Sugiyama, T., Cheng, J., Saeki, Y., Tanaka, K., Becker, T., Beckmann, R., & Inada, T.
- Affiliations
- Tohoku University (JP)
- Center for Integrated Protein Science Munich (DE)
- Tokyo Metropolitan Institute of Medical Science (JP)
- Corresponding author
- Beckmann, Roland
- Inada, Toshifumi
- ORCID
- Venue
- The EMBO Journal
- Published
- 2019-01-04
- Volume
- 38
- Issue
- 5
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC6396155
- OpenAlex
- W2908095537
- Cited by
- 315
- References
- 51
- Citations by year
- 2026: 41 · 2025: 36 · 2024: 40 · 2023: 51 · 2022: 27 · 2021: 45 · 2020: 49 · 2019: 25 · 2018: 1
- FWCI
- 12.07
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Takeda Foundation
- German Research Council (FOR1805, BE1814/15‐1)
- Center for Integrated Protein Science Munich
- Graduate School of Quantitative Biosciences Munich
- MEXT|Japan Society for the Promotion of Science (26116003)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- ribosome stalling, ribosome-associated quality control, no-go decay, K63-linked ubiquitination, mRNA quality control
- MeSH terms
- Ribosomal Proteins, Ribosomes, RNA, Messenger, Saccharomyces cerevisiae, Protein Biosynthesis, Cryoelectron Microscopy, RNA Stability, Ubiquitin, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, Ubiquitination
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