Human SEIPIN Binds Anionic Phospholipids.

Abstract:

: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.

journal_name

Dev Cell

journal_title

Developmental cell

authors

Yan R,Qian H,Lukmantara I,Gao M,Du X,Yan N,Yang H

doi

10.1016/j.devcel.2018.09.010

subject

Has Abstract

pub_date

2018-10-22 00:00:00

pages

248-256.e4

issue

2

eissn

1534-5807

issn

1878-1551

pii

S1534-5807(18)30739-1

journal_volume

47

pub_type

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