Evidence map›Paper›PMID 34625558›Full record

ArticleNature communications2021

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

Yoel A Klug, Justin C Deme, Robin A Corey, Mike F Renne, Phillip J Stansfeld, Susan M Lea, Pedro Carvalho

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.7field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

49 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Lipid Droplet Dynamics in Alcoholic Steatohepatitis.The American journal of pathology · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Targeting Seipin to Alleviate Hepatic Steatosis in Zebrafish (Danio Rerio).Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  15. Article
  16. Article
  17. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Essential Biology of Lipid Droplets.Annual review of biochemistry · 2025
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Yoel A KlugSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0001-9775-3161
Justin C Deme *Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Robin A Corey *Department of Biochemistry, University of Oxford, Oxford, UK.
Mike F Renne *Sir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0003-0508-2298
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-8800-7669
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford, UK. susan.lea@nih.gov.ORCID 0000-0001-9287-8053
Pedro CarvalhoSir William Dunn School of Pathology, University of Oxford, Oxford, UK. pedro.carvalho@path.ox.ac.uk.ORCID 0000-0002-9691-5277
University of Oxford · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P01948X/1Biotechnology and Biological Sciences Research Council BB/R002517/1Biotechnology and Biological Sciences Research Council BB/R018375/1Biotechnology and Biological Sciences Research Council BB/S003339/1Medical Research Council MR/S009213/1Medical Research Council MR/S021264/1Wellcome Trust 201536Wellcome Trust 202642/Z/16/ZWellcome Trust 208361/Z/17/ZWellcome Trust 219477/Z/19/Z
6 · The paper itself

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.

Indexed as

Endoplasmic ReticulumGTP-Binding Protein gamma SubunitsLipid DropletsMembrane LipidsMembrane ProteinsMitochondrial ProteinsModels, MolecularMolecular Dynamics SimulationPhospholipidsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTriglyceridesGTP-Binding Protein gamma SubunitsLDB16 protein, S cerevisiaeMembrane LipidsMembrane ProteinsMitochondrial ProteinsPhospholipidsSaccharomyces cerevisiae Proteinsseipin protein, S cerevisiaeTriglycerides

Identifiers

PMID34625558
PMCPMC8501077
OpenAlexW3203857810

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.