Evidence map›Paper›PMID 41451945›Full record

ArticleFEBS letters2026

Crosstalk between the ribosome quality control-associated E3 ubiquitin ligases LTN1 and RNF10.

Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada

Abstract read
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In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Yuxi HuangDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.
Satoshi HashimotoDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.ORCID 0000-0002-6445-1885
Sota ItoDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.ORCID 0009-0007-7498-0012
Chisato KikuguchiDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.
Miho HoshiDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.
Kiyoshi YamaguchiDivision of Clinical Genome Research, Center for Experimental Medicine and Systems Biology, The Institute of Medical Science, The University of Tokyo, Minato-ku, Japan.
Yoichi FurukawaDivision of Clinical Genome Research, Center for Experimental Medicine and Systems Biology, The Institute of Medical Science, The University of Tokyo, Minato-ku, Japan.
Toru SuzukiDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.
Toshifumi InadaDivision of RNA and Gene Regulation, Institute of Medical Science, The University of Tokyo, Minato-Ku, Japan.ORCID 0000-0002-2695-588X

Funding

Japan Agency for Medical Research and Development JP223fa627001Japan Agency for Medical Research and Development JP23gm1110010Japan Society for the Promotion of Science 21H05277Japan Society for the Promotion of Science 22H00401Japan Society for the Promotion of Science 25H00007Japan Society for the Promotion of Science 25K18399Japan Society for the Promotion of Science JP19H05281Mitsubishi FoundationTakeda Science Foundation
6 · The paper itself

Abstract

During gene expression, ribosome stalling frequently occurs and can lead to detrimental effects on cellular homeostasis. Several quality control mechanisms, including ribosome-associated quality control (RQC) and nonfunctional ribosomal RNA decay (NRD), have been identified to resolve these aberrant translation events. While the molecular mechanisms of each pathway have been extensively characterized, the mechanisms underlying the mutual regulation of the expression of pathway factors remain to be elucidated. Here, we employed a series of knockout mouse and human cell lines to investigate the crosstalk between translational quality control factors. Our findings revealed that the E3 ubiquitin ligase LTN1 suppresses expression of the E3 ubiquitin ligase RNF10 in a manner dependent on the RING domain of LTN1. This discovery offers new insights into the coordination of translational surveillance pathways.

Indexed as

RibosomesUbiquitin-Protein LigasesAnimalsHEK293 CellsHumansMiceMice, KnockoutProtein BiosynthesisUbiquitin-Protein LigasesLTN1ribosome ubiquitinationRING domainRNF10RQC

Identifiers

PMID41451945
PMCPMC13075771

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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.