ArticleGenes & development2025
The ribosome-associated quality control factor TCF25 imposes K48 specificity on Listerin-mediated ubiquitination of nascent chains by binding and specifically orienting the acceptor ubiquitin.
Article in Genes & development, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Crosstalk between the ribosome quality control-associated E3 ubiquitin ligases LTN1 and RNF10.FEBS letters · 2026Article
- Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026Review
- Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026Review
- Chromosome duplication causes premature aging via defects in ribosome quality control.PLoS biology · 2025Article
- Large-scale genome-wide association analysis reveals candidate genes in yak body size traits.BMC genomics · 2025Article
- TCF25 serves as a nutrient sensor to orchestrate metabolic adaptation and cell death by enhancing lysosomal acidification under glucose starvation.Cell reports · 2025Article
- Mechanism of nascent chain removal by the ribosome-associated quality control complex.Nature communications · 2025Article
- Transcription factor 25 modulates gametocytogenesis and ribosome biogenesis in the malaria parasiteFrontiers in cellular and infection microbiology · 2025Article
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Abstract
Polypeptides arising from interrupted translation undergo proteasomal degradation by the ribosome-associated quality control (RQC) pathway. The ASC-1 complex splits stalled ribosomes into 40S subunits and nascent chain-tRNA-associated 60S subunits (60S RNCs). 60S RNCs associate with NEMF that promotes recruitment of the RING-type E3 ubiquitin (Ub) ligase Listerin (Ltn1 in yeast), which ubiquitinates nascent chains. RING-type E3s mediate the transfer of Ub directly from the E2∼Ub conjugate, implying that the specificity of Ub linkage is determined by the given E2. Listerin is most efficient when it is paired with promiscuous Ube2D E2s. We previously found that TCF25 (Rqc1 in yeast) can impose K48 specificity on Listerin paired with Ube2D E2s. To determine the mechanism of TCF25's action, we combined functional biochemical studies and AlphaFold3 modeling and now report that TCF25 specifically interacts with the RING domain of Listerin and the acceptor ubiquitin (Ub
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