Mechanisms and functions of ribosome-associated protein quality control
Open accessAbstract
The stalling of ribosomes during protein synthesis results in the production of truncated polypeptides that can have deleterious effects on cells and therefore must be eliminated. In eukaryotes, this function is carried out by a dedicated surveillance mechanism known as ribosome-associated protein quality control (RQC). The E3 ubiquitin ligase Ltn1 (listerin in mammals) plays a key part in RQC by targeting the aberrant nascent polypeptides for proteasomal degradation. Consistent with having an important protein quality control function, mutations in listerin cause neurodegeneration in mice. Ltn1/listerin is part of the multisubunit RQC complex, and recent findings have revealed that the Rqc2 subunit of this complex catalyses the formation of carboxy-terminal alanine and threonine tails (CAT tails), which are extensions of nascent chains known to either facilitate substrate ubiquitylation and targeting for degradation or induce protein aggregation. RQC, originally described for quality control on ribosomes translating cytosolic proteins, is now known to also have a role on the surfaces of the endoplasmic reticulum and mitochondria. This Review describes our current knowledge on RQC mechanisms, highlighting key features of Ltn1/listerin action that provide a paradigm for understanding how E3 ligases operate in protein quality control in general, and discusses how defects in this pathway may compromise cellular function and lead to disease.
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Ribosome collisions are detected by surveillance mechanisms including the E3 ubiquitin ligase ZNF598, which marks defective translational complexes for resolution and degradation.
“These events are detected by surveillance mechanisms that include the E3 ubiquitin ligase ZNF598, which helps mark defective translational complexes for resolution and degradation [208,209].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [208]
The Introduction (page unavailable) says ribosome stalling initiates surveillance that targets nascent proteins for degradation, and the References list identifies ZNF598 as an E3 ligase involved in ribosome quality control and 40S ubiquitylation. Our copy does not establish that ZNF598 detects ribosome collisions specifically; the Substrate recognition and ubiquitylation section instead identifies Ltn1 as marking ribosome-associated nascent chains for degradation. (LLM, conf=0.78)
Experimental — accuracy not yet measuredIf 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 [208]
The ‘Activation of stress signalling’ section (page unavailable) reports that compromised ribosome-associated quality control activates Hsf1 stress signalling. ‘Ribosome sequestration’ (page unavailable) says unresolved stalled ribosomes can potentially reduce translational efficiency. The paper does not link anabolic signalling or insufficient recovery to increased translational errors, or say that stress responses cause the reduction in efficiency. (LLM, conf=0.87)
Experimental — accuracy not yet measuredBy limiting persistence of stalled ribosomes, RQC contributes to proteome quality and reduces accumulation of aberrant translation products.
“By limiting the persistence of stalled ribosomes, RQC contributes to proteome quality and reduces the accumulation of aberrant translation products [208,211].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [208]
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“Ribosome biogenesis therefore needs to be considered alongside the systems responsible for monitoring ribosomal function, removing damaged components, and preserving translational fidelity [64,208].”
Influential
- Authors
- Joazeiro, C. A. P.
- Affiliations
- Heidelberg University (DE)
- Corresponding author
- Joazeiro, Claudio A. P.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2019-04-02
- Volume
- 20
- Issue
- 6
- Pages
- 368-383
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC7138134
- OpenAlex
- W2927984698
- Cited by
- 456
- References
- 118
- Citations by year
- 2026: 72 · 2025: 52 · 2024: 67 · 2023: 72 · 2022: 55 · 2021: 67 · 2020: 54 · 2019: 17
- FWCI
- 4.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS075719, R01NS102414)
- 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 › Heat shock proteins research
- Keywords
- ribosome stalling, truncated protein, E3 ubiquitin ligase, proteasomal degradation, protein quality control, neurodegeneration, endoplasmic reticulum, mitochondria, protein aggregation
- MeSH terms
- Animals, Cytosol, Endoplasmic Reticulum, Humans, Mitochondria, Ribosomes, Protein Biosynthesis, Ubiquitin-Protein Ligases, Mice, Ubiquitination, Proteolysis
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