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TitleHuman SEIPIN Binds Anionic Phospholipids.
Journal, issue, pagesDev Cell, Vol. 47, Issue 2, Page 248-256.e4, Year 2018
Publish dateOct 22, 2018
AuthorsRenhong Yan / Hongwu Qian / Ivan Lukmantara / Mingming Gao / Ximing Du / Nieng Yan / Hongyuan Yang /
PubMed AbstractThe biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a ...The biogenesis of lipid droplets (LDs) and the development of adipocytes are two key aspects of mammalian fat storage. SEIPIN, an integral membrane protein of the endoplasmic reticulum (ER), plays a critical role in both LD formation and adipogenesis. The molecular function of SEIPIN, however, has yet to be elucidated. Here, we report the cryogenic electron microscopy structure of human SEIPIN at 3.8 Å resolution. SEIPIN exists as an undecamer, and this oligomerization state is critical for its physiological function. The evolutionarily conserved lumenal domain of SEIPIN forms an eight-stranded β sandwich fold. Both full-length SEIPIN and its lumenal domain can bind anionic phospholipids including phosphatidic acid. Our results suggest that SEIPIN forms a scaffold that helps maintain phospholipid homeostasis and surface tension of the ER.
External linksDev Cell / PubMed:30293840
MethodsEM (single particle)
Resolution3.8 Å
Structure data

8909

6ds5

EMDB-8909, PDB-6ds5:
Cryo EM structure of human SEIPIN
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • homo sapiens (human)
KeywordsLIPID BINDING PROTEIN / Lipid droplets / adipogenesis

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