RNA G-quadruplexes control mitochondria-localized mRNA translation and energy metabolism

Leïla Dumas, Sauyeun Shin, Quentin Rigaud, Marie Cargnello, Beatriz Hernández-Suárez, Pauline Herviou, Nathalie Saint-Laurent, Marjorie Leduc, Morgane Gall, David Monchaud, Erik Dassi (), Anne Cammas () and Stefania Millevoi ()
Additional contact information
Leïla Dumas: Université Toulouse III-Paul Sabatier
Sauyeun Shin: Université Toulouse III-Paul Sabatier
Quentin Rigaud: Université Toulouse III-Paul Sabatier
Marie Cargnello: Université Toulouse III-Paul Sabatier
Beatriz Hernández-Suárez: Université Toulouse III-Paul Sabatier
Pauline Herviou: Université Toulouse III-Paul Sabatier
Nathalie Saint-Laurent: Université Toulouse III-Paul Sabatier
Marjorie Leduc: Proteom’IC facility, Université Paris Cité, CNRS, INSERM Institut Cochin
Morgane Gall: Proteom’IC facility, Université Paris Cité, CNRS, INSERM Institut Cochin
David Monchaud: Institut de Chimie Moléculaire (ICMUB), UBFC Dijon CNRS UMR6302
Erik Dassi: University of Trento
Anne Cammas: Université Toulouse III-Paul Sabatier
Stefania Millevoi: Université Toulouse III-Paul Sabatier

Nature Communications, 2025, vol. 16, issue 1, 1-22

Abstract: Abstract Cancer cells rely on mitochondria for their bioenergetic supply and macromolecule synthesis. Central to mitochondrial function is the regulation of mitochondrial protein synthesis, which primarily depends on the cytoplasmic translation of nuclear-encoded mitochondrial mRNAs whose protein products are imported into mitochondria. Despite the growing evidence that mitochondrial protein synthesis contributes to the onset and progression of cancer, and can thus offer new opportunities for cancer therapy, knowledge of the underlying molecular mechanisms remains limited. Here, we show that RNA G-quadruplexes (RG4s) regulate mitochondrial function by modulating cytoplasmic mRNA translation of nuclear-encoded mitochondrial proteins. Our data support a model whereby the RG4 folding dynamics, under the control of oncogenic signaling and modulated by small molecule ligands or RG4-binding proteins, modifies mitochondria-localized cytoplasmic protein synthesis. Ultimately, this impairs mitochondrial functions, affecting energy metabolism and consequently cancer cell proliferation.

Date: 2025
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DOI: 10.1038/s41467-025-58118-5

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