Evidence map›Paper›PMID 33674387›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Seipin accumulates and traps diacylglycerols and triglycerides in its ring-like structure.

Valeria Zoni, Rasha Khaddaj, Ivan Lukmantara, Wataru Shinoda, Hongyuan Yang, Roger Schneiter, Stefano Vanni

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

66 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Targeting Seipin to Alleviate Hepatic Steatosis in Zebrafish (Danio Rerio).Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  15. Article
  16. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Review

6 more citing papers are in PubMed but not listed here.

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 3 institutions in 3 countries.

Valeria ZoniDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Rasha KhaddajDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Ivan LukmantaraSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia.
Wataru ShinodaDepartment of Materials Chemistry, Nagoya University, Chikusa-ku, 464-8603 Nagoya, Japan.ORCID 0000-0002-3388-9227
Hongyuan YangSchool of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW 2052, Australia.ORCID 0000-0002-8482-6031
Roger SchneiterDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Stefano VanniDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland; stefano.vanni@unifr.ch.ORCID 0000-0003-2146-1140
University of Fribourg · CHUNSW Sydney · AUNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid droplets (LDs) are intracellular organelles responsible for lipid storage, and they emerge from the endoplasmic reticulum (ER) upon the accumulation of neutral lipids, mostly triglycerides (TG), between the two leaflets of the ER membrane. LD biogenesis takes place at ER sites that are marked by the protein seipin, which subsequently recruits additional proteins to catalyze LD formation. Deletion of seipin, however, does not abolish LD biogenesis, and its precise role in controlling LD assembly remains unclear. Here, we use molecular dynamics simulations to investigate the molecular mechanism through which seipin promotes LD formation. We find that seipin clusters TG, as well as its precursor diacylglycerol, inside its unconventional ring-like oligomeric structure and that both its luminal and transmembrane regions contribute to this process. This mechanism is abolished upon mutations of polar residues involved in protein-TG interactions into hydrophobic residues. Our results suggest that seipin remodels the membrane of specific ER sites to prime them for LD biogenesis.

Indexed as

DiglyceridesGTP-Binding Protein gamma SubunitsLipid DropletsMolecular Dynamics SimulationTriglyceridesCell LineHumansBSCL2 protein, humanDiglyceridesGTP-Binding Protein gamma SubunitsTriglyceridesendoplasmic reticulumlipid dropletslipid membranesmolecular dynamicsseipin

Identifiers

PMID33674387
PMCPMC7958289
OpenAlexW3135262287

What OpenQuestion holds

Textmetadata
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.