Znf598-mediated Rps10/eS10 ubiquitination contributes to the ribosome ubiquitination dynamics during zebrafish development

Ugajin, Nozomi; Imami, Koshi; Takada, Hiraku; Ishihama, Yasushi; Chiba, Shinobu; Mishima, Yuichiro

doi:10.1261/rna.079633.123

Cited by 5 publications

(2 citation statements)

References 76 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A zebrafish znf598 mutant strain with an 11-base deletion in exon 1, predicted to cause frameshifting at the middle of the RING domain, was generated previously [37]. Embryos lacking maternal and zygotic znf598 activity (MZ znf598 ) are defective in mRNA decay induced by the ribosome stall sequence of hCMV gp48 uORF2 and cannot ubiquitinate Rps10/eS10 in response to translational stresses [37,54].…”

Section: Resultsmentioning

confidence: 99%

Translation of zinc finger domains induces ribosome collision and Znf598-dependent mRNA decay in vertebrates

Ishibashi

Shichino

Han

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

Quality control of translation is crucial for maintaining cellular and organismal homeostasis. Obstacles in translation elongation induce ribosome collision, which is monitored by multiple sensor mechanisms. The E3 ubiquitin ligase ZNF598 recognizes collided ribosomes, triggering ribosome-associated quality control (RQC) to rescue stalled ribosomes and no-go decay (NGD) to degrade stall-prone mRNAs in eukaryotes. However, the role of RQC and NGD in maintaining the translational homeostasis of endogenous mRNAs has remained largely unclear. In this study, we investigated endogenous substrate mRNAs of NGD using the maternal-to-zygotic transition (MZT) of zebrafish embryos as a model system. Combining RNA-Seq analysis of znf598 mutant embryos with disome profiling and reporter assays, we revealed that mRNAs encoding the C2H2-type zinc finger domain (C2H2-ZF) frequently cause ribosome collisions and induce NGD during the MZT. Furthermore, we showed that mRNAs encoding C2H2-ZF are degraded by ZNF598 in human cells. Our results suggest that NGD maintains the quality of the translatome during protein evolution and animal development by mitigating the risk of ribosome collision at the abundantly present C2H2-ZF mRNA sequences.

show abstract

Section: Resultsmentioning

confidence: 99%

Translation of zinc finger domains induces ribosome collision and Znf598-dependent mRNA decay in vertebrates

Ishibashi

Shichino

Han

et al. 2023

Preprint

Self Cite

View full text Add to dashboard Cite

show abstract

“…[57] In eukaryotes, Hel2/ZNF598 interacts with collided ribosomes and ubiquitylates 40S ribosomal proteins eS10 (Rps10) and uS10 (Rps20) in the stalled ribosomes. [58,59] Another ubiquitin ligase RNF10 ubiquitylates Rps2 and Rps3 on stalled ribosomes in a ZNF598dependent manner. [60] During the integrated stress response, RNF10 ubiquitylates 40S ribosomes in a ZNF598-independent way.…”

Section: Dormant Ribosomes In Ribosome Preservationmentioning

confidence: 99%

Ribosomal dormancy at the nexus of ribosome homeostasis and protein synthesis

Koli,

Shetty

2024

BioEssays

View full text Add to dashboard Cite

Dormancy or hibernation is a non‐proliferative state of cells with low metabolic activity and gene expression. Dormant cells sequester ribosomes in a translationally inactive state, called dormant/hibernating ribosomes. These dormant ribosomes are important for the preservation of ribosomes and translation shut‐off. While recent studies attempted to elucidate their modes of formation, the regulation and roles of the diverse dormant ribosomal populations are still largely understudied. The mechanistic details of the formation of dormant ribosomes in stress and especially their disassembly during recovery remain elusive. In this review, we discuss the roles of dormant ribosomes and their potential regulatory mechanisms. Furthermore, we highlight the paradigms that need to be answered in the field of ribosomal dormancy.

show abstract