ArticleNature structural & molecular biology2025
ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- ACAD10 encodes two orphan enzymes in the ether lipid biosynthetic and salvage pathways.bioRxiv : the preprint server for biology · 2026Article
- Gestational Feed Restriction Induces Differential Expression of Novel Long Non-Coding RNAs in Offspring Skeletal Muscle.Animal genetics · 2026Article
- Bacterial ubiquitin ligase engineered for small molecule and protein target identification.The EMBO journal · 2026Article
- Integrative multi-omics uncovers skeletal muscle enhancer programming of cardiorespiratory fitness.bioRxiv : the preprint server for biology · 2025Article
- ACAD10 and ACAD11 enable mammalian 4-hydroxy acid lipid catabolism.Nature structural & molecular biology · 2025Article
- Haptoglobin and Glutamine Synthetase May Biomark Cachexia Induced by Antiacute Myeloid Leukaemia Chemotherapy.Journal of cachexia, sarcopenia and muscle · 2025Article
- Integrative Transcriptomic and Metabolomic Analysis of Muscle and Liver Reveals Key Molecular Pathways Influencing Growth Traits in Zhedong White Geese.Animals : an open access journal from MDPI · 2025Article
- Genome-Wide Identification and Functional Characterization of the Acyl-CoA Dehydrogenase (ACAD) Family inInternational journal of molecular sciences · 2025Article
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19 authors.
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Abstract
Fatty acid β-oxidation is a central catabolic pathway with broad health implications. However, various fatty acids, including 4-hydroxy acids (4-HAs), are largely incompatible with β-oxidation machinery before being modified. Here we reveal that two atypical acyl-CoA dehydrogenases, ACAD10 and ACAD11, drive 4-HA catabolism in mice. Unlike other ACADs, ACAD10 and ACAD11 feature kinase domains that phosphorylate the 4-hydroxy position as a requisite step in converting 4-hydroxyacyl-CoAs into conventional 2-enoyl-CoAs. Through cryo-electron microscopy and molecular modeling, we identified an atypical dehydrogenase binding pocket capable of accommodating this phosphorylated intermediate. We further show that ACAD10 is mitochondrial and necessary for catabolizing shorter-chain 4-HAs, whereas ACAD11 is peroxisomal and enables longer-chain 4-HA catabolism. Mice lacking ACAD11 accumulate 4-HAs in their plasma and females are susceptible to body weight and fat gain, concurrent with decreased adipocyte differentiation and adipokine expression. Collectively, we present that ACAD10 and ACAD11 are the primary gatekeepers of mammalian 4-HA catabolism.
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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.