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Lookup NU author(s): Gailing Ma, Diego Manni, Dr Marco Trevisan, Professor Gavin RichardsonORCiD, Dr Daniel ErskineORCiD, Professor Viktor KorolchukORCiD, Dr Tetsushi Kataura
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2026 The Author(s). FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. Maintenance of protein homeostasis requires coordination between protein synthesis and degradation, yet whether autophagy directly controls translational machinery remains unclear. Here we explored whether autophagy maintains translational fidelity. Proteomic analysis of ubiquitin-enriched fractions and p62-associated proteins in autophagy-deficient tissue confirmed previous studies identifying ribosomal proteins and RNA-binding factors among candidate autophagy cargo. Pharmacological or genetic impairment of autophagy increased translational errors, particularly during oxidative stress. Components of the translational machinery localised to LC3-positive autophagic structures and accumulated in human brain tissue affected by neurodegeneration. These findings support a hypothesis in which autophagy preserves protein synthesis quality by removing damaged translational machinery. We term this proposed mechanism translophagy, potentially linking autophagy dysfunction, oxidative stress and the aberrant proteins in neurodegenerative disease.
Author(s): Korolchuk MV, Ma G, Antrobus R, Manni D, Trevisan-Herraz M, Khwaja M, Brown M, Richardson GD, Komatsu M, Erskine D, Korolchuk VI, Kataura T
Publication type: Article
Publication status: Published
Journal: FEBS Letters
Year: 2026
Pages: Epub ahead of print
Online publication date: 27/08/2026
Acceptance date: 24/07/2026
Date deposited: 07/09/2026
ISSN (print): 0014-5793
ISSN (electronic): 1873-3468
Publisher: John Wiley and Sons Inc.
URL: https://doi.org/10.1002/1873-3468.70448
DOI: 10.1002/1873-3468.70448
Data Access Statement: The data supporting the findings of this study are available from the corresponding authors viktor.korolchuk@newcastle.ac.uk and tkataura@md.tsukuba.ac.jp upon reasonable request.
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