Evidence map›Paper›PMID 41120337›Full record

ArticleScientific reports2025

Disrupting mitochondrial β-oxidation by depletion of HADHA impairs primary ciliogenesis.

Joon Bum Kim, Yong Hwan Kim, Seong Hyun Kim, Hyejin Hyung, Jun Hee So, Daeun Park, Na Yeon Park, Dong Kyu Choi, Ji-Eun Bae, Dong-Hyung Cho

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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

10 authors.

Joon Bum KimSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Yong Hwan KimSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Seong Hyun KimSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Hyejin HyungSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Jun Hee SoSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Daeun ParkSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Na Yeon ParkOrganelle Institute, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Dong Kyu ChoiSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea.
Ji-Eun BaeOrganelle Institute, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea. jieunbae@knu.ac.kr.
Dong-Hyung ChoSchool of Life Sciences, BK21 FOUR KNU Creative BioResearch Group, Kyungpook National University, 80 Daehakro, Bukgu, Daegu, 41566, Republic of Korea. dhcho@knu.ac.kr.

Funding

Korea Institute for Advancement of Technology (KIAT) P0025489Ministry of Education RS-2024-00463344Ministry of Science & ICT RS-2024-00338475
6 · The paper itself

Abstract

Primary cilia are dynamic signaling hubs essential for cell homeostasis, and defects in ciliogenesis underpin various genetic disorders. Alpha-hydroxyacyl-CoA dehydrogenase (HADHA), a subunit of the mitochondrial trifunctional enzyme, is crucial for long-chain fatty acid β-oxidation and acetyl-CoA production. Although it was recently demonstrated that lipid metabolism modulates primary ciliogenesis, the connection between mitochondrial β-oxidation and primary cilia remains largely unexplored. Here, we report that HADHA dysfunction markedly impairs primary ciliogenesis and disrupts cilia-dependent signaling. Loss of HADHA reduces both ciliary frequency and length, accompanied by decreased levels of key ciliary signaling mediators. Reintroduction of wild-type HADHA in HADHA knockout cells rescues these defects, whereas its dehydrogenase deficiency mutant (E510Q) fails to restore either normal cilia formation or ciliary signaling. Notably, supplementation with sodium acetate, which resupplies intracellular acetyl-CoA, effectively rescues primary cilium in HADHA-deficient cells. Importantly, this acetate-mediated rescue implicates a potential therapeutic strategy for HADHA-related disorders, supporting the translational relevance of modulating acetyl-CoA levels to restore ciliary function. These findings suggest a relevant link between mitochondrial β-oxidation and primary ciliogenesis, highlighting acetyl-CoA as a potential therapeutic target for disorders related to HADHA deficiency.

Indexed as

CiliaMitochondriaAcetyl Coenzyme AAnimalsHumansMiceOxidation-ReductionSignal TransductionAcetyl Coenzyme AAcetyl-CoACiliopathyHADHAPrimary ciliaβ-oxidation

Identifiers

PMID41120337
PMCPMC12541092

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LicenceCC BY-NC-ND
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Registered trials

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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.