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TitleSeipin forms a flexible cage at lipid droplet formation sites.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 3, Page 194-202, Year 2022
Publish dateFeb 24, 2022
AuthorsHenning 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 AbstractLipid 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.
External linksNat Struct Mol Biol / PubMed:35210614 / PubMed Central
MethodsEM (single particle)
Resolution3.45 Å
Structure data

24674

7rsl

EMDB-24674, PDB-7rsl:
Seipin forms a flexible cage at lipid droplet formation sites
Method: EM (single particle) / Resolution: 3.45 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMEMBRANE PROTEIN / lipid droplets / lipid droplet formation / complex / endoplasmic reticulum / fat storage

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