Saltar al contenido
Merck

Human SEIPIN Binds Anionic Phospholipids.

Developmental cell (2018-10-09)
Renhong Yan, Hongwu Qian, Ivan Lukmantara, Mingming Gao, Ximing Du, Nieng Yan, Hongyuan Yang
RESUMEN

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.

MATERIALES
Referencia del producto
Marca
Descripción del producto

Sigma-Aldrich
Digitonina, Used as non-ionic detergent
Sigma-Aldrich
Ácido oleico, BioReagent, suitable for cell culture
Supelco
Colesterol, Pharmaceutical Secondary Standard; Certified Reference Material