ArticleMolecular biology of the cell2022
ER-localized phosphatidylethanolamine synthase plays a conserved role in lipid droplet formation.
Article in Molecular biology of the cell, 2022. 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, 15 citations in OpenAlex.
- PCYT2 inhibits lipid accumulation via the notch signaling pathway in chicken primary hepatocytes.Poultry science · 2026Article
- The Role of ATG8 in Promoting Lipid Accumulation in the Oleaginous FungusJournal of fungi (Basel, Switzerland) · 2026Article
- Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026Review
- Effects of surfactin stress on gene expression and pathological changes in Spodoptera litura.Scientific reports · 2024Article
- Membrane protein Bcsdr2 mediates biofilm integrity, hyphal growth and virulence of Botrytis cinerea.Applied microbiology and biotechnology · 2024Article
- A dynamin superfamily-like pseudoenzyme coordinates with MICOS to promote cristae architecture.Current biology : CB · 2024Article
- Chemical inhibition of phosphatidylcholine biogenesis reveals its role in mitochondrial division.iScience · 2024Article
- A DRP-like pseudoenzyme coordinates with MICOS to promote cristae architecture.bioRxiv : the preprint server for biology · 2023Article
- Completion of mitochondrial division requires the intermembrane space protein Mdi1/Atg44.The Journal of cell biology · 2023Article
- An intermembrane space protein facilitates completion of mitochondrial division in yeast.bioRxiv : the preprint server for biology · 2023Article
- Fundamental roles for inter-organelle communication in aging.Biochemical Society transactions · 2022Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The asymmetric distribution of phospholipids in membranes is a fundamental principle of cellular compartmentalization and organization. Phosphatidylethanolamine (PE), a nonbilayer phospholipid that contributes to organelle shape and function, is synthesized at several subcellular localizations via semiredundant pathways. Previously, we demonstrated in budding yeast that the PE synthase Psd1, which primarily operates on the mitochondrial inner membrane, is additionally targeted to the ER. While ER-localized Psd1 is required to support cellular growth in the absence of redundant pathways, its physiological function is unclear. We now demonstrate that ER-localized Psd1 sublocalizes on the ER to lipid droplet (LD) attachment sites and show it is specifically required for normal LD formation. We also find that the role of phosphatidylserine decarboxylase (PSD) enzymes in LD formation is conserved in other organisms. Thus we have identified PSD enzymes as novel regulators of LDs and demonstrate that both mitochondria and LDs in yeast are organized and shaped by the spatial positioning of a single PE synthesis enzyme.
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Registered trials
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.