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-Structure paper
タイトル | Seipin forms a flexible cage at lipid droplet formation sites. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 3, Page 194-202, Year 2022 |
掲載日 | 2022年2月24日 |
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 / |
PubMed 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. |
リンク | Nat Struct Mol Biol / PubMed:35210614 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.45 Å |
構造データ | EMDB-24674, PDB-7rsl: |
由来 |
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キーワード | MEMBRANE PROTEIN / lipid droplets / lipid droplet formation / complex / endoplasmic reticulum / fat storage |