ArticleProceedings of the National Academy of Sciences of the United States of America2015
Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 166 citations in OpenAlex.
- COP1 regulates the abundance and stability of the Arabidopsis retromer protein AtVPS29 via the proteasome pathway.Plant signaling & behavior · 2026Article
- Depot-dependent peroxisome response in the rat white adipose tissue under hypothyroidism.European journal of histochemistry : EJH · 2026Article
- Lipid droplet proteome plasticity in plant evolution, growth and development, and response to stress.Journal of experimental botany · 2026Review
- Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026Review
- Understanding the dynamic nature of plant lipid anabolic and catabolic metabolism is key to sustainable oilseed engineering.The New phytologist · 2026Review
- Lipid droplets at the interface of plant defense and pathogen exploitation.Frontiers in plant science · 2026Review
- Quantitative proteomic analysis of Arabidopsis thaliana with different levels of phospholipid:diacylglycerol acyltransferase1 expression.BMC genomics · 2025Article
- Peroxisomal-dependent signalling and dynamics modulate plant stress responses: reactive oxygen and nitrogen species as key molecules.Journal of experimental botany · 2025Review
- Diatom triacylglycerol metabolism: from carbon fixation to lipid droplet degradation.Biological reviews of the Cambridge Philosophical Society · 2025Review
- Lipid droplets as cell fate determinants in skeletal muscle.Trends in endocrinology and metabolism: TEM · 2025Review
- Retromer protein VPS29 plays a crucial and positive role in the sumoylation system mediated by E3 SUMO ligase SIZ1.The Plant journal : for cell and molecular biology · 2025Article
- The Atypical Pectin Methylesterase Family Member PME31 Promotes Seedling Lipid Droplet Utilization.Plant direct · 2025Article
- Lipid droplets in plants: turnover and stress responses.Frontiers in plant science · 2025Review
- Mitochondria and Lipid Droplets: Focus on the Molecular Structure of Contact Sites in the Pathogenesis of Metabolic Syndrome.Current medicinal chemistry · 2025Review
- Exploiting lipid droplet metabolic pathway to foster lipid production: oleosin in focus.Plant cell reports · 2024Review
- Global impacts of peroxisome and pexophagy dysfunction revealed through multi-omics analyses of lon2 and atg2 mutants.The Plant journal : for cell and molecular biology · 2024Article
- Functional multi-organelle units control inflammatory lipid metabolism of macrophages.Nature cell biology · 2024Article
- Identification of triacylglycerol remodeling mechanism to synthesize unusual fatty acid containing oils.Nature communications · 2024Article
- Developmental pleiotropy of SDP1 from seedling to mature stages in B. napus.Plant molecular biology · 2024Article
- Arabidopsis retromer subunit AtVPS29 is involved in SLY1-mediated gibberellin signaling.Plant cell reports · 2024Article
20 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid droplets/oil bodies (OBs) are lipid-storage organelles that play a crucial role as an energy resource in a variety of eukaryotic cells. Lipid stores are mobilized in the case of food deprivation or high energy demands--for example, during certain developmental processes in animals and plants. OB degradation is achieved by lipases that hydrolyze triacylglycerols (TAGs) into free fatty acids and glycerol. In the model plant Arabidopsis thaliana, Sugar-Dependent 1 (SDP1) was identified as the major TAG lipase involved in lipid reserve mobilization during seedling establishment. Although the enzymatic activity of SDP1 is associated with the membrane of OBs, its targeting to the OB surface remains uncharacterized. Here we demonstrate that the core retromer, a complex involved in protein trafficking, participates in OB biogenesis, lipid store degradation, and SDP1 localization to OBs. We also report an as-yet-undescribed mechanism for lipase transport in eukaryotic cells, with SDP1 being first localized to the peroxisome membrane at early stages of seedling growth and then possibly moving to the OB surface through peroxisome tubulations. Finally, we show that the timely transfer of SDP1 to the OB membrane requires a functional core retromer. In addition to revealing previously unidentified functions of the retromer complex in plant cells, our work provides unanticipated evidence for the role of peroxisome dynamics in interorganelle communication and protein transport.
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