Evidence map›Paper›PMID 39863576›Full record

ArticleNature communications2025

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 de Oliveira, Bretton Laboret, Songjie Chen, Ruiqi Jian, Lihua Jiang and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Raptor and Drp1 Function Synthetically to Control Hypoxic Death and the Mitochondrial Network in Caenorhabditis elegans.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Review
  5. Review
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

16 authors.

Foozhan TahmasebiniaDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.
Yinglu TangDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.ORCID http://orcid.org/0000-0002-1022-7554
Rushi TangDepartment of Pharmacy and Pharmaceutical Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
Yi ZhangDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.
Will BondererDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.
Maisa de OliveiraDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.
Bretton LaboretDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA.
Songjie ChenDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0002-9568-5705
Ruiqi JianDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0003-2406-5303
Lihua JiangDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.
Michael SnyderDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0003-0784-7987
Chun-Hong ChenNational Institute of Infectious Diseases and Vaccinology, NHRI, Miaoli, 350401, Taiwan.ORCID http://orcid.org/0000-0002-3028-5508
Yawei ShenDepartment of Biological Sciences, Clemson University, Clemson, SC, 29634, USA.ORCID http://orcid.org/0000-0003-2595-7995
Qing LiuDepartment of Biological Sciences, Clemson University, Clemson, SC, 29634, USA.ORCID http://orcid.org/0000-0002-1765-8517
Boxiang LiuDepartment of Pharmacy and Pharmaceutical Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore. boxiangliu@nus.edu.sg.ORCID http://orcid.org/0000-0002-2595-4463
Zhihao WuDepartment of Biological Sciences, Dedman College of Humanities and Sciences, Southern Methodist University, Dallas, TX, 75275, USA. zhihaowu@smu.edu.ORCID http://orcid.org/0000-0003-3080-5769

Funding

Statistical Methods for Gene Regulatory Analysis From Single Cell Genomics DataP20GM139769 · NIGMS · CLEMSON UNIVERSITY · PI ANHOLT, ROBERT R. H, ARNO, GAVIN · 2021 to 2025
$10.8M
Decipher the Organization of a Multilayered Cellular Quality Control NetworkR35GM150190 · NIGMS · SOUTHERN METHODIST UNIVERSITY · PI Zhihao Wu · 2023 to 2026
$1.4M
THE ROLE OF HYDROGEN GAS IN HEALTH AND DISEASER15AG067470 · NIA · SOUTHERN METHODIST UNIVERSITY · PI RADYUK, SVETLANA NIKOLAEVNA · 2021 to 2021
$437k
Cancer Prevention and Research Institute of Texas (Cancer Prevention Research Institute of Texas) RP210068NIA NIH HHS R15 AG067470NIGMS NIH HHS P20 GM139769NIGMS NIH HHS R35 GM150190U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM150190U.S. Department of Health & Human Services | NIH | National Institute on Aging (U.S. National Institute on Aging) R15AG067470
6 · The paper itself

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.

Indexed as

Endoplasmic ReticulumMitochondriaMitochondrial DynamicsRibosome Subunits, Small, EukaryoticHEK293 CellsHeLa CellsHumansMechanistic Target of Rapamycin Complex 1Poly-ADP-Ribose Binding ProteinsRNA HelicasesMechanistic Target of Rapamycin Complex 1Poly-ADP-Ribose Binding ProteinsRNA Helicases

Identifiers

PMID39863576
PMCPMC11762756

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.