ArticleMetabolism: clinical and experimental2026
Mitochondrial phosphopantetheinylation is required for oxidative metabolism.
Article in Metabolism: clinical and experimental, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Integrated expression profiling reveals molecular crosstalk between CFTR, FASN, FRAP (mTOR), and BANK1 in hepatocellular carcinoma.Scientific reports · 2026Article
- Cells Engage Endogenous Malonate Synthesis to Drive Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026Article
- Functional partitioning of lipoic acid decouples cellular abundance from mitochondrial utilization.bioRxiv : the preprint server for biology · 2026Article
- Molecular subtype of recurrent implantation failure reveals distinct endometrial etiology of female infertility.Journal of translational medicine · 2025Article
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10 authors.
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Abstract
4'-Phosphopantetheinyl (4'PP) groups are essential co-factors added to target proteins by phosphopantetheinyl transferase (PPTase) enzymes. Although mitochondrial 4'PP-modified proteins have been described for decades, a mitochondrially-localized PPTase has never been found in mammals. We discovered that the cytoplasmic PPTase aminoadipate semialdehyde dehydrogenase phosphopantetheinyl transferase (AASDHPPT) is required for mitochondrial respiration and oxidative metabolism. Loss of AASDHPPT results in failed 4'PP modification of the mitochondrial acyl carrier protein and blunted activity of the mitochondrial fatty acid synthesis (mtFAS) pathway. We found that in addition to its cytoplasmic localization, AASDHPPT localizes to the mitochondrial matrix via an N-terminal mitochondrial targeting sequence contained within the first 20 amino acids of the protein. Our data show that this novel mitochondrial localization of AASDHPPT is required to support mtFAS activity and oxidative metabolism. We further identify five variants of uncertain significance in AASDHPPT that are likely pathogenic in humans due to loss of mtFAS activity.
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