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The seipin complex Fld1/Ldb16 stabilizes ER-lipid droplet contact sites.

J. Cell Biol.2015 Nov 23;211(4):829-44. Epub 2015 Nov 16
Alexandra Grippa 1 , Laura Buxó 1 , Gabriel Mora 1 , Charlotta Funaya 2 , Fatima-Zahra Idrissi 1 , Francesco Mancuso 1 , Raul Gomez 1 , Júlia Muntanyà 3 , Eduard Sabidó 1 , Pedro Carvalho 4
Alexandra Grippa 1 , Laura Buxó 1 , Gabriel Mora 1 , Charlotta Funaya 2 , Fatima-Zahra Idrissi 1 , Francesco Mancuso 1 , Raul Gomez 1 , Júlia Muntanyà 3 , Eduard Sabidó 1 , Pedro Carvalho 4
+ et al

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Author information
  • 1 Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
  • 2 Electron Microscopy Core Facility, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
  • 3 Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain.
  • 4 Centre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain pedro.carvalho@crg.eu.
全文

摘要


Lipid droplets (LDs) are storage organelles consisting of a neutral lipid core surrounded by a phospholipid monolayer and a set of LD-specific proteins. Most LD components are synthesized in the endoplasmic reticulum (ER), an organelle that is often physically connected with LDs. How LD identity is established while maintaining biochemical and physical connections with the ER is not known. Here, we show that the yeast seipin Fld1, in complex with the ER membrane protein Ldb16, prevents equilibration of ER and LD surface components by stabilizing the contact sites between the two organelles. In the absence of the Fld1/Ldb16 complex, assembly of LDs results in phospholipid packing defects leading to aberrant distribution of lipid-binding proteins and abnormal LDs. We propose that the Fld1/Ldb16 complex facilitates the establishment of LD identity by acting as a diffusion barrier at the ER-LD contact sites.