ArticleBiochimica et biophysica acta. Molecular and cell biology of lipids2020
Vps39 is required for ethanolamine-stimulated elevation in mitochondrial phosphatidylethanolamine.
Article in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Mitochondrial dysfunction and lipid dysregulation in yeast lacking phosphatidylserine.Molecular biology of the cell · 2025Article
- Article
- Chemical inhibition of phosphatidylcholine biogenesis reveals its role in mitochondrial division.iScience · 2024Article
- Mitochondrial phospholipid metabolism in health and disease.Journal of cell science · 2023Article
- Phospholipase D3 degrades mitochondrial DNA to regulate nucleotide signaling and APP metabolism.Nature communications · 2023Article
- Molecular species selectivity of lipid transport creates a mitochondrial sink for di-unsaturated phospholipids.The EMBO journal · 2022Article
- SGPL1 stimulates VPS39 recruitment to the mitochondria in MICU1 deficient cells.Molecular metabolism · 2022Article
- Vam6/Vps39/TRAP1-domain proteins influence vacuolar morphology, iron acquisition and virulence in Cryptococcus neoformans.Cellular microbiology · 2021Article
- Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole.Molecular biology of the cell · 2021Article
- Phospholipid ebb and flow makes mitochondria go.The Journal of cell biology · 2020Review
- Choline restores respiration in Psd1-deficient yeast by replenishing mitochondrial phosphatidylethanolamine.The Journal of biological chemistryArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Mitochondrial membrane biogenesis requires the import of phospholipids; however, the molecular mechanisms underlying this process remain elusive. Recent work has implicated membrane contact sites between the mitochondria, endoplasmic reticulum (ER), and vacuole in phospholipid transport. Utilizing a genetic approach focused on these membrane contact site proteins, we have discovered a 'moonlighting' role of the membrane contact site and vesicular fusion protein, Vps39, in phosphatidylethanolamine (PE) transport to the mitochondria. We show that the deletion of Vps39 prevents ethanolamine-stimulated elevation of mitochondrial PE levels without affecting PE biosynthesis in the ER or its transport to other sub-cellular organelles. The loss of Vps39 did not alter the levels of other mitochondrial phospholipids that are biosynthesized ex situ, implying a PE-specific role of Vps39. The abundance of Vps39 and its recruitment to the mitochondria and the ER is dependent on PE levels in each of these organelles, directly implicating Vps39 in the PE transport process. Deletion of essential subunits of Vps39-containing complexes, vCLAMP and HOPS, did not abrogate ethanolamine-stimulated PE elevation in the mitochondria, suggesting an independent role of Vps39 in intracellular PE trafficking. Our work thus identifies Vps39 as a novel player in ethanolamine-stimulated PE transport to the mitochondria.
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