The Library
Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex
Tools
Tools
Tools
Klug, Yoel A., Deme, Justin C., Corey, Robin A., Renne, Mike F., Stansfeld, Phillip J., Lea, Susan M. and Caralho, Pedro (2021) Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex. Nature Communications, 12 . 5892. doi:10.1038/s41467-021-26162-6 ISSN 2041-1723.
|
PDF
WRAP-Mechanism-lipid-droplet-formation-yeast-Sei1-Ldb16-2021.pdf - Published Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (3490Kb) | Preview |
|
![[img]](https://wrap.warwick.ac.uk/style/images/fileicons/application_pdf.png) |
PDF
WRAP-Mechanism-lipid-droplet-formation-yeast-Sei1-Ldb16-2021.pdf - Accepted Version Embargoed item. Restricted access to Repository staff only - Requires a PDF viewer. Download (34Mb) |
Official URL: https://doi.org/10.1038/s41467-021-26162-6
Abstract
Lipid droplets (LDs) are universal lipid storage organelles with a core of neutral lipids, such as triacylglycerols, surrounded by a phospholipid monolayer. This unique architecture is generated during LD biogenesis at endoplasmic reticulum (ER) sites marked by Seipin, a conserved membrane protein mutated in lipodystrophy. Here structural, biochemical and molecular dynamics simulation approaches reveal the mechanism of LD formation by the yeast Seipin Sei1 and its membrane partner Ldb16. We show that Sei1 luminal domain assembles a homooligomeric ring, which, in contrast to other Seipins, is unable to concentrate triacylglycerol. Instead, Sei1 positions Ldb16, which concentrates triacylglycerol within the Sei1 ring through critical hydroxyl residues. Triacylglycerol recruitment to the complex is further promoted by Sei1 transmembrane segments, which also control Ldb16 stability. Thus, we propose that LD assembly by the Sei1/Ldb16 complex, and likely other Seipins, requires sequential triacylglycerol-concentrating steps via distinct elements in the ER membrane and lumen.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QP Physiology | ||||||||||||||||||||||||||||||||||||||||||
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Lipids, Membrane lipids, Membrane proteins -- Research | ||||||||||||||||||||||||||||||||||||||||||
| Journal or Publication Title: | Nature Communications | ||||||||||||||||||||||||||||||||||||||||||
| Publisher: | Nature Publishing Group | ||||||||||||||||||||||||||||||||||||||||||
| ISSN: | 2041-1723 | ||||||||||||||||||||||||||||||||||||||||||
| Official Date: | 8 October 2021 | ||||||||||||||||||||||||||||||||||||||||||
| Dates: |
|
||||||||||||||||||||||||||||||||||||||||||
| Volume: | 12 | ||||||||||||||||||||||||||||||||||||||||||
| Article Number: | 5892 | ||||||||||||||||||||||||||||||||||||||||||
| DOI: | 10.1038/s41467-021-26162-6 | ||||||||||||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||||||||||||||||||||||||||
| Date of first compliant deposit: | 24 September 2021 | ||||||||||||||||||||||||||||||||||||||||||
| Date of first compliant Open Access: | 11 October 2021 | ||||||||||||||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
|
||||||||||||||||||||||||||||||||||||||||||
| Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
