Evidence map›Paper›PMID 41728289›Full record

ArticlemedRxiv : the preprint server for health sciences2026

Cooperative Architecture of Mitochondrial Proteome Homeostasis.

Patrick Forny, Merima Forny, Andrew J Smith, Andrew Y Sung, Kaixian Liu, David J Pagliarini

Abstract readPreprint
In one paragraph

Article in medRxiv : the preprint server for health sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

6 authors.

Patrick FornyDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.ORCID 0000-0003-1877-2976
Merima FornyDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Andrew J SmithDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Andrew Y SungDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Kaixian LiuDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
David J PagliariniDepartment of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

Funding

WU P&FP30DK020579 · NIDDK · WASHINGTON UNIVERSITY · PI David W Piston · 2013 to 2026
$27.1M
Biology of Aging and Age-Related Diseases Training GrantT32AG000213 · NIA · UNIVERSITY OF WISCONSIN-MADISON · PI Rozalyn M. Anderson, Sanjay Asthana · 1991 to 2026
$9.9M
Integrated Training For Physician-ScientistsT32GM140935 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Anna Huttenlocher, Jeniel E Nett · 2021 to 2026
$6.5M
Systems-to-structure approaches for defining mitochondrial protein functionR35GM131795 · NIGMS · WASHINGTON UNIVERSITY · PI David J Pagliarini · 2019 to 2026
$4.8M
NIA NIH HHS T32 AG000213NIDDK NIH HHS P30 DK020579NIGMS NIH HHS R35 GM131795NIGMS NIH HHS T32 GM140935
6 · The paper itself

Abstract

Mitochondria are semi-autonomous organelles whose generation and maintenance demand precise expression, processing, and assembly of >1,000 proteins encoded across two genomes. To explore this cooperativity, we performed multiomic analyses on >200 cell lines harboring mitochondrial gene perturbations, generating >26M molecular measurements. Our data reveal that mitochondrial proteome homeostasis is heavily influenced by post-transcriptional processes. Through nearest neighbor analyses, we reveal diverse protein activities undergirding this regulation, including MDH2's regulation of MT-ND3 transcription via FASTKD1 binding and CLPP's processing of the mitoribosomal assembly factor MALSU1, which we establish as a disease gene. Through entropy analysis, we reveal unexpectedly heterogeneous protein-level variability across complexes and use complexome profiling to identify new complex-specific membership, including C15orf61's association with complex V. We further observe substantial mtDNA copy number variation, notably upon disruption of the disease-related cobalamin biosynthesis protein MMADHC. Together, we establish new protein functions and provide a multilayered view into mitochondrial proteome regulation.

Indexed as

C15orf61CLPPCRISPR knockout screenFASTKD1MALSU1MDH2MitochondriaMitochondrial proteome homeostasisMMADHCmultiomic profilingNADK2

Identifiers

PMID41728289
PMCPMC12919160

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.