期刊
JOURNAL OF CELL BIOLOGY
卷 217, 期 12, 页码 4080-4091出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201809067
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资金
- National Institutes of Health [1R01GM123089, 1R01GM124348-01, 1R01GM097194]
- American Heart Association postdoctoral fellowship [18POST34030308]
- Deutsche Forschungsgemeinschaft research fellowship [AR1164/1-1]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM097194, R01GM123089, R01GM124348] Funding Source: NIH RePORTER
Metabolic energy is stored in cells primarily as triacylglycerols in lipid droplets (LDs), and LD dysregulation leads to metabolic diseases. The formation of monolayer-bound LDs from the endoplasmic reticulum (ER) bilayer is poorly understood, but the ER protein seipin is essential to this process. In this study, we report a cryo-electron microscopy structure and functional characterization of Drosophila melanogaster seipin. The structure reveals a ring-shaped dodecamer with the luminal domain of each monomer resolved at similar to 4.0 angstrom. Each luminal domain monomer exhibits two distinctive features: a hydrophobic helix (HH) positioned toward the ER bilayer and a beta-sandwich domain with structural similarity to lipid-binding proteins. This structure and our functional testing in cells suggest a model in which seipin oligomers initially detect forming LDs in the ER via HHs and subsequently act as membrane anchors to enable lipid transfer and LD growth.
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