ArticleThe Journal of cell biology2025
Phosphatidic acid drives spatiotemporal distribution of Pex30 at ER-LD contact sites.
Article in The Journal of cell biology, 2025. 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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Who cites it
4 citing papers in PubMed.
- Protocol to determine in vitro lipid-protein interactions using liposome flotation assay.STAR protocols · 2026Article
- Seipin-defined ER sites undergo distinct enrichment of factors for the biogenesis of sterol ester rich lipid droplets.iScience · 2026Article
- The reticulon homology domain of Pex30 generates membrane curvature at ER subdomains for lipid droplet biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Role of Pex31 in metabolic adaptation of the nucleus-vacuole junction.Journal of cell science · 2025Article
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8 authors.
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Abstract
Lipid droplets (LDs) are ubiquitous neutral lipid storage organelles that form at discrete subdomains in the ER bilayer. The assembly of these ER subdomains and the mechanism by which proteins are recruited to them is poorly understood. Here, we investigate the spatiotemporal distribution of Pex30 at the ER-LD membrane contact sites (MCSs). Pex30, an ER membrane-shaping protein, has a reticulon homology domain, a dysferlin (DysF) domain, and a Duf4196 domain. Deletion of SEI1, which codes for seipin, a highly conserved protein required for LD biogenesis, results in accumulation of Pex30 and phosphatidic acid (PA) at ER-LD contact sites. We show that PA recruits Pex30 at ER subdomains by binding to the DysF domain. The distribution of Pex30 as well as PA is also affected by phosphatidylcholine (PC) levels. We propose that PA regulates the spatiotemporal distribution of Pex30 at ER subdomains that plays a critical role in driving the formation of LDs in the ER membrane.
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