The 40S ribosomal subunit recycling complex modulates mitochondrial dynamics and endoplasmic reticulum - mitochondria tethering at mitochondrial fission/fusion hotspots

Foozhan Tahmasebinia, Yinglu Tang, Rushi Tang, Yi Zhang, Will Bonderer, Maisa Oliveira, Bretton Laboret, Songjie Chen, Ruiqi Jian, Lihua Jiang, Michael Snyder, Chun-Hong Chen, Yawei Shen, Qing Liu, Boxiang Liu () and Zhihao Wu ()
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Foozhan Tahmasebinia: Southern Methodist University
Yinglu Tang: Southern Methodist University
Rushi Tang: National University of Singapore
Yi Zhang: Southern Methodist University
Will Bonderer: Southern Methodist University
Maisa Oliveira: Southern Methodist University
Bretton Laboret: Southern Methodist University
Songjie Chen: Stanford University School of Medicine
Ruiqi Jian: Stanford University School of Medicine
Lihua Jiang: Stanford University School of Medicine
Michael Snyder: Stanford University School of Medicine
Chun-Hong Chen: NHRI
Yawei Shen: Clemson University
Qing Liu: Clemson University
Boxiang Liu: National University of Singapore
Zhihao Wu: Southern Methodist University

Nature Communications, 2025, vol. 16, issue 1, 1-24

Abstract: Abstract The 40S ribosomal subunit recycling pathway is an integral link in the cellular quality control network, occurring after translational errors have been corrected by the ribosome-associated quality control (RQC) machinery. Despite our understanding of its role, the impact of translation quality control on cellular metabolism remains poorly understood. Here, we reveal a conserved role of the 40S ribosomal subunit recycling (USP10-G3BP1) complex in regulating mitochondrial dynamics and function. The complex binds to fission-fusion proteins located at mitochondrial hotspots, regulating the functional assembly of endoplasmic reticulum-mitochondria contact sites (ERMCSs). Furthermore, it alters the activity of mTORC1/2 pathways, suggesting a link between quality control and energy fluctuations. Effective communication is essential for resolving proteostasis-related stresses. Our study illustrates that the USP10-G3BP1 complex acts as a hub that interacts with various pathways to adapt to environmental stimuli promptly. It advances our molecular understanding of RQC regulation and helps explain the pathogenesis of human proteostasis and mitochondrial dysfunction diseases.

Date: 2025
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DOI: 10.1038/s41467-025-56346-3

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