Evidence map›Paper›PMID 40501579›Full record

ArticlebioRxiv : the preprint server for biology2025

EXOSC3 S1-domain variants implicated in PCH1b alter RNA exosome cap subunit abundance and thermal stability disrupting rRNA processing and targeting of AU-rich mRNA.

Avery M Runnebohm, H R Sagara Wijeratne, Monica P Barron, Whitney R Smith-Kinnaman, James D Rooney, Sarah A Peck Justice, Lauryn A Cureton, Annalise Holland, Homa Ghalei, Stephane Pelletier and 3 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. 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

13 authors.

Avery M RunnebohmDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0001-6798-6407
H R Sagara WijeratneDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0002-8209-5626
Monica P BarronDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0001-8841-6614
Whitney R Smith-KinnamanDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0003-1174-0920
James D RooneyDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.
Sarah A Peck JusticeDepartment of Biology, Marian University, Indianapolis, IN.ORCID 0000-0002-0658-732X
Lauryn A CuretonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, USA.
Annalise HollandDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, USA.
Homa GhaleiDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, USA.ORCID 0000-0003-0168-4654
Stephane PelletierDepartment of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0002-1127-0212
Emma H DoudDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0003-0049-0073
Jonah Z VilseckDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0001-7076-8996
Amber L MosleyDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN.ORCID 0000-0001-5822-2894

Funding

Tumor Microenvironment and Metastasis ProgramP30CA082709 · NCI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI David W Clapp · 1999 to 2026
$59.3M
Quality Assurance and Quality Control Project Management: Improving Submissions and Study Conduct in the Human Subjects Research Prior Approval ProcessUL1TR002529 · NCATS · INDIANA UNIVERSITY INDIANAPOLIS · PI MOE, SHARON M, WIEHE, SARAH ELIZABETH · 2018 to 2022
$27.2M
Indiana Medical Scientist/Engineer Training ProgramT32GM148382 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI Benjamin Gaston, Emily K Sims · 2023 to 2026
$3.9M
Biogenesis of macromolecular machines for post-transcriptional regulation of translationR35GM138123 · NIGMS · EMORY UNIVERSITY · PI Homa Ghalei · 2020 to 2026
$3.0M
Tackling Multifaceted Drug Design Problems with Lambda Dynamics Based TechnologiesR35GM146888 · NIGMS · INDIANA UNIVERSITY INDIANAPOLIS · PI JONAH VILSECK · 2022 to 2026
$1.9M
Thermal proteome profiling for analysis of protein sequence variants in human genetic diseaseR01NS121550 · NINDS · INDIANA UNIVERSITY INDIANAPOLIS · PI MOSLEY, AMBER L. · 2021 to 2025
$1.9M
Pediatric and Adult Translational Cancer Drug Discovery and Development Training Program (PACT-D3)T32CA272370 · NCI · INDIANA UNIVERSITY INDIANAPOLIS · PI David W Clapp, Mark R. Kelley · 2023 to 2026
$569k
Proteomic and functional analysis of missense variants of APOE associated with Alzheimer disease riskF30AG079580 · NIA · INDIANA UNIVERSITY INDIANAPOLIS · PI WIJERATNE, HR SAGARA · 2022 to 2025
$159k
NCATS NIH HHS UL1 TR002529NCI NIH HHS P30 CA082709NCI NIH HHS T32 CA272370NIA NIH HHS F30 AG079580NIGMS NIH HHS R35 GM138123NIGMS NIH HHS R35 GM146888NIGMS NIH HHS T32 GM148382NINDS NIH HHS R01 NS121550
6 · The paper itself

Abstract

Missense variants in EXOSC3, an RNA exosome subunit, have been identified in patients with PCH1b. We investigated three missense variants in the S1 domain of EXOSC3, including one variant of uncertain significance (VUS) and two pathogenic variants (hence S1 variants). EXOSC3 S1 variant cell lines were generated using CRISPR-Cas9 resulting in widespread proteome changes including decreases in some RNA exosome subunits paired with increases in the catalytic subunit DIS3. Thermal stability, analyzed by PISA, revealed extensive destabilization of RNA exosome cap subunits and the cap-associated exonuclease EXOSC10. Functionally, S1 variants altered rRNA processing with corresponding protein compensation observed in rRNA processing proteins outside the RNA exosome. Exogenous overexpression of EXOSC3 rescues many molecular defects caused by S1 variants suggesting that protein destabilization and turnover strongly contribute to molecular defects. Overall, our findings define the mechanisms through which cells respond to EXOSC3 S1 variant disruption of RNA processing homeostasis.

Identifiers

PMID40501579
PMCPMC12154690

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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.