IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v12y2021i1d10.1038_s41467-021-26162-6.html
   My bibliography  Save this article

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

Author

Listed:
  • Yoel A. Klug

    (University of Oxford)

  • Justin C. Deme

    (University of Oxford
    National Cancer Institute)

  • Robin A. Corey

    (University of Oxford)

  • Mike F. Renne

    (University of Oxford)

  • Phillip J. Stansfeld

    (University of Oxford
    University of Warwick)

  • Susan M. Lea

    (University of Oxford
    National Cancer Institute)

  • Pedro Carvalho

    (University of Oxford)

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.

Suggested Citation

  • Yoel A. Klug & Justin C. Deme & Robin A. Corey & Mike F. Renne & Phillip J. Stansfeld & Susan M. Lea & Pedro Carvalho, 2021. "Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26162-6
    DOI: 10.1038/s41467-021-26162-6
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-021-26162-6
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-021-26162-6?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Calvin Dumesnil & Lauri Vanharanta & Xavier Prasanna & Mohyeddine Omrane & Maxime Carpentier & Apoorva Bhapkar & Giray Enkavi & Veijo T. Salo & Ilpo Vattulainen & Elina Ikonen & Abdou Rachid Thiam, 2023. "Cholesterol esters form supercooled lipid droplets whose nucleation is facilitated by triacylglycerols," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Ravi Dhiman & Rehani S. Perera & Chetan S. Poojari & Haakon T. A. Wiedemann & Reinhard Kappl & Christopher W. M. Kay & Jochen S. Hub & Bianca Schrul, 2024. "Hairpin protein partitioning from the ER to lipid droplets involves major structural rearrangements," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26162-6. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.