ArticleNature communications2019
Molecular interactions between Hel2 and RNA supporting ribosome-associated quality control.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 45 citations in OpenAlex.
- TOR-NOT4 signalling couples translation to co-translational quality control in plants.Nature communications · 2026Article
- Yeast elongation factor homolog New1 protects a subset of mRNAs from degradation by no-go decay.Nucleic acids research · 2026Article
- Rapid remodeling of NTP levels enables immediate translational adaptation to energy stress in yeast.Molecular cell · 2025Article
- Article
- Stalled disomes marked by Hel2-dependent ubiquitin chains undergo Ubp2/Ubp3-mediated deubiquitination upon translational run-off.Communications biology · 2025Article
- Ribosomal collision is not a prerequisite for ZNF598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ASCC.Nucleic acids research · 2024Article
- Transcriptional profile of ribosome-associated quality control components and their associated phenotypes in mammalian cells.Scientific reports · 2024Article
- The ribosome quality control factor Asc1 determines the fate of HSP70 mRNA on and off the ribosome.Nucleic acids research · 2023Article
- Interaction of the La-related protein Slf1 with colliding ribosomes maintains translation of oxidative-stress responsive mRNAs.Nucleic acids research · 2023Article
- Review
- The human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism.Molecular cell · 2022Article
- Canary in a coal mine: collided ribosomes as sensors of cellular conditions.Trends in biochemical sciences · 2022Review
- Ending a bad start: Triggers and mechanisms of co-translational protein degradation.Frontiers in molecular biosciences · 2022Review
- A Multi-Perspective Proximity View on the Dynamic Head Region of the Ribosomal 40S Subunit.International journal of molecular sciences · 2021Article
- Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase.Molecular cell · 2021Article
- Tools for Assessing Translation inJournal of fungi (Basel, Switzerland) · 2021Review
- The expression of Rpb10, a small subunit common to RNA polymerases, is modulated by the R3H domain-containing Rbs1 protein and the Upf1 helicase.Nucleic acids research · 2020Article
- Stress-Induced Translation Inhibition through Rapid Displacement of Scanning Initiation Factors.Molecular cell · 2020Article
- Detection and Degradation of Stalled Nascent Chains via Ribosome-Associated Quality Control.Annual review of biochemistry · 2020Review
- Genome-wide Survey of Ribosome Collision.Cell reports · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 3 countries.
Funding
Abstract
Ribosome-associated quality control (RQC) pathways monitor and respond to ribosome stalling. Using in vivo UV-crosslinking and mass spectrometry, we identified a C-terminal region in Hel2/Rqt1 as an RNA binding domain. Complementary crosslinking and sequencing data for Hel2 revealed binding to 18S rRNA and translated mRNAs. Hel2 preferentially bound mRNAs upstream and downstream of the stop codon. C-terminal truncation of Hel2 abolished the major 18S crosslink and polysome association, and altered mRNA binding. HEL2 deletion caused loss of RQC and, we report here, no-go decay (NGD), with comparable effects for Hel2 truncation including the RNA-binding site. Asc1 acts upstream of Hel2 in RQC and asc1∆ impaired Hel2 binding to 18S and mRNA. In conclusion: Hel2 is recruited or stabilized on translating 40S ribosomal subunits by interactions with 18S rRNA and Asc1. This 18S interaction is required for Hel2 function in RQC and NGD. Hel2 probably interacts with mRNA during translation termination.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.