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Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex

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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.

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Official URL: https://doi.org/10.1038/s41467-021-26162-6

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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:
DateEvent
8 October 2021Published
21 September 2021Accepted
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:
Project/Grant IDRIOXX Funder NameFunder ID
BB/R018375/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
202642/Z/16/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
201536Wellcome Trusthttp://dx.doi.org/10.13039/100010269
WL160052Edward Penley Abraham Cephalosporin TrustUNSPECIFIED
WL160052[RS] Royal Societyhttp://dx.doi.org/10.13039/501100000288
WL160052Wolfson Foundationhttp://dx.doi.org/10.13039/501100001320
219477/Z/19/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
BB/P01948X/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
MR/S009213/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
EP/L000253/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
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