ArticleNature communications2026
Ashwin and FAM98 paralogs define nuclear and cytoplasmic RNA ligase complexes for tRNA biogenesis.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Structural framework for the assembly of the human tRNA ligase complex.Nature communications · 2026Article
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
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Authors and funding
6 authors.
Funding
Abstract
The tRNA ligase complex (tRNA-LC) seals tRNA exon halves in the nucleus during pre-tRNA splicing and XBP1-mRNA exons in the cytoplasm as part of the unfolded protein response (UPR). This dual function requires the tRNA-LC to be either nuclear or cytoplasmic. Here, we reveal that Ashwin (ASW), the vertebrate-specific subunit of the tRNA-LC, serves as its nuclear import factor. ASW contains a dual nuclear localisation signal (NLS) which, upon disruption, leads to the retention of the tRNA-LC in the cytoplasm, impairing pre-tRNA splicing with the consequent accumulation of 5' tRNA fragments. We also show that the tRNA-LC exists in three forms, depending on which FAM98 paralog is bound, either FAM98A, FAM98B or FAM98C. ASW interacts exclusively with the FAM98B-containing complex, ensuring its nuclear localization for tRNA biogenesis. Attaching an NLS to RTCB, the catalytic and indispensable tRNA-LC subunit, rescues pre-tRNA splicing in cells depleted of ASW. We hypothesize that vertebrates evolved ASW to localize a sub-population of tRNA-LC to the nucleus, while using FAM98 paralogs to retain a fraction of RTCB in the cytoplasm to splice XBP1-mRNA during UPR.
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