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REVIEW ARTICLE

Toward an understanding of cancer-associated ribosomal protein mutations

Mikael S. Lindström1*
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1 Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden
Tumor Discovery, 025230042 https://doi.org/10.36922/TD025230042
Received: 5 June 2025 | Revised: 2 September 2025 | Accepted: 8 September 2025 | Published online: 3 October 2025
© 2025 by the Author(s). This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution 4.0 International License ( https://creativecommons.org/licenses/by/4.0/ )
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Abstract

Ribosomal proteins (RPs) are essential structural and functional components of the ribosome, and their disruption during embryogenesis generally results in embryonic lethality. Nevertheless, cancer genomes frequently harbor somatic missense mutations and gene deletions in RP genes in patterns that suggest selective advantages, often linked to inactivation of the tumor suppressor protein p53 pathway. This review discusses the landscape of RP mutations in cancer and their mechanistic consequences. RP mutations are detected across multiple malignancies, including glioblastoma, melanoma, T-cell acute lymphoblastic leukemia, as well as in congenital ribosomopathies, such as Diamond-Blackfan anemia, which confer an elevated lifetime risk of developing cancer. Cancer-associated RP mutations disturb ribosome homeostasis, compromise translational fidelity, and trigger proteotoxic and ribosomal stress, yet without halting tumor growth. Some RP mutants occupy structurally sensitive positions within the ribosome, altering mRNA selectivity and quality control. In turn, cancer cells may adapt through compensatory mechanisms, including the upregulation of RP paralogs, activation of proteostasis regulators, and rewiring of stress response pathways. Rather than a loss-of-function event, an RP mutation may create a persistent ribosomal disequilibrium that fundamentally alters cellular functions. Such changes in a cancer cell could generate interesting therapeutic vulnerabilities and targets, such as dependence on stress signaling, proteasome activity, or RP paralog expression.

Keywords
Ribosome biogenesis
Ribosomal protein
p53
Cancer
Ribosomal stress
Funding
None.
Conflict of interest
Mikael S. Lindström is an Editorial Board Member of this journal, but was not in any way involved in the editorial and peer-review process conducted for this paper, directly or indirectly.
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Tumor Discovery, Electronic ISSN: 2810-9775 Print ISSN: 3060-8597, Published by AccScience Publishing
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