National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM124348
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM084210
米国
German Research Foundation (DFG)
AR1164/1-1
米国
American Heart Association
POST34030308
米国
Howard Hughes Medical Institute (HHMI)
米国
引用
ジャーナル: Nat Struct Mol Biol / 年: 2022 タイトル: Seipin forms a flexible cage at lipid droplet formation sites. 著者: Henning Arlt / Xuewu Sui / Brayden Folger / Carson Adams / Xiao Chen / Roman Remme / Fred A Hamprecht / Frank DiMaio / Maofu Liao / Joel M Goodman / Robert V Farese / Tobias C Walther / 要旨: Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, ...Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding.
名称: Seipin dimer / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: all 詳細: Dimer of seipin monomers in transmembrane segment conformation A and B (chain A and B). That was used to build the oligomer consisting of 5 dimers (10 monomers).