title: Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies.
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.
authors.affiliation: Laboratoire de Reproduction et Développement des Plantes, Unité Mixte de Recherche 5667 Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1, 69364 Lyon Cedex 07, France; and.
authors.forename: Nelcy
authors.initials: N
authors.lastname: Thazar-Poulot
authors.affiliation: Institut Jean-Pierre Bourgin, Unité Mixte de Recherche 1318 Institut National de la Recherche Agronomique-AgroParisTech, Équipe de Recherche Labellisée CNRS 3559, Institut National de la Recherche Agronomique Centre de Versailles-Grignon, 78026 Versailles Cedex, France.
authors.forename: Martine
authors.initials: M
authors.lastname: Miquel
authors.affiliation: Laboratoire de Reproduction et Développement des Plantes, Unité Mixte de Recherche 5667 Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1, 69364 Lyon Cedex 07, France; and thierry.gaude@ens-lyon.fr isabelle.fobis-loisy@ens-lyon.fr.
authors.forename: Isabelle
authors.initials: I
authors.lastname: Fobis-Loisy
authors.affiliation: Laboratoire de Reproduction et Développement des Plantes, Unité Mixte de Recherche 5667 Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Ecole Normale Supérieure de Lyon, Université Claude Bernard Lyon 1, 69364 Lyon Cedex 07, France; and thierry.gaude@ens-lyon.fr isabelle.fobis-loisy@ens-lyon.fr.
authors.forename: Thierry
authors.initials: T
authors.lastname: Gaude
mesh_terms: D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000378:metabolism; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D017343:Genes, Plant; D018525:Germination; D008049:Lipase / Q000378:metabolism; D066292:Lipid Droplets / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry; D018613:Microscopy, Confocal; D009154:Mutation; D010100:Oxygen / Q000737:chemistry; D020675:Peroxisomes / Q000737:chemistry* / Q000378:metabolism; D010641:Phenotype; D018517:Plant Roots / Q000378:metabolism; D021381:Protein Transport; D036226:Seedlings / Q000254:growth & development; D012639:Seeds / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D008055:Lipids; D002265:Carboxylic Ester Hydrolases; D008049:Lipase; C510423:SDP1 protein, Arabidopsis; D010100:Oxygen
keywords: SDP1 lipase; oil bodies; peroxisome; protein trafficking; retromer