Cited by 87RNA and protein synthesis mechanismsRNA Research and SplicingRNA modifications and cancer

A cellular handbook for collided ribosomes: Surveillance pathways and collision types

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Meydan, Sezen, Guydosh, Nicholas R.·2021·Current Genetics

Abstract

Translating ribosomes slow down or completely stall when they encounter obstacles on mRNAs. Such events can lead to ribosomes colliding with each other and forming complexes of two (disome), three (trisome) or more ribosomes. While these events can activate surveillance pathways, it has been unclear if collisions are common on endogenous mRNAs and whether they are usually detected by these cellular pathways. Recent genome-wide surveys of collisions revealed widespread distribution of disomes and trisomes across endogenous mRNAs in eukaryotic cells. Several studies further hinted that the recognition of collisions and response to them by multiple surveillance pathways depend on the context and duration of the ribosome stalling. This review considers recent efforts in the identification of endogenous ribosome collisions and cellular pathways dedicated to sense their severity. We further discuss the potential role of collided ribosomes in modulating co-translational events and contributing to cellular homeostasis.

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Crossref · 10.1007/s00294-020-01111-w

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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 [209]

    In “Multiple surveillance pathways detect ribosome collisions” (page not provided), the paper describes ribosome stalling or collisions activating an integrated stress response that blocks translation initiation. It does not connect that response to anabolic signaling, insufficient recovery, or an increase in translational errors, so it supports only the stress-response and translation-inhibition portion of the claim. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • 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].”

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Authors
Meydan, S., & Guydosh, N. R.
Affiliations
National Institutes of Health (US)
Corresponding author
Guydosh, Nicholas R.
Venue
Current Genetics
Published
2020-10-12
Volume
67
Issue
1
Pages
19-26
ISSN
  • 0172-8083 (ISSN-L)
  • 1432-0983
OpenAlex
W3092101222
Cited by
87
References
77
Citations by year
2026: 12 · 2025: 14 · 2024: 20 · 2023: 21 · 2022: 12 · 2021: 8
FWCI
0.98
Type
journal article
Language
en
Open access
Locations
  • Current Genetics (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK075132)
  • National Institute of General Medical Sciences (1FI2GM137845)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords
ribosome collisions, ribosome stalling, endogenous mRNA, ribosome-associated quality control, eukaryotic translation
MeSH terms
Ribosomes, RNA, Messenger, Saccharomyces cerevisiae, Protein Biosynthesis, Saccharomyces cerevisiae Proteins, Ubiquitination

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