Evidence map›Paper›PMID 35938957›Full record

ArticleThe Journal of cell biology2022

Seipin concentrates distinct neutral lipids via interactions with their acyl chain carboxyl esters.

Mike F Renne, Robin A Corey, Joana Veríssimo Ferreira, Phillip J Stansfeld, Pedro Carvalho

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. The evolving landscape of ER-LD contact sites.Frontiers in cell and developmental biology · 2024
    Review
  13. Review
  14. Concept of lipid droplet biogenesis.European journal of cell biology · 2023
    Review
  15. Review
  16. Structure and function of lipid droplet assembly complexes.Current opinion in structural biology · 2023
    Review
  17. Article
  18. Article
  19. Seipin-still a mysterious protein?Frontiers in cell and developmental biology · 2023
    Review
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

5 authors at 2 institutions in 1 country.

Mike F RenneSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0003-0508-2298
Robin A CoreyDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0003-1820-7993
Joana Veríssimo FerreiraSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0003-4341-1654
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0001-880-7669
Pedro CarvalhoSir William Dunn School of Pathology, University of Oxford, Oxford, 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/S009213/1Wellcome Trust 202642/Z/16/ZWellcome Trust 208361/Z/17/Z
6 · The paper itself

Abstract

Lipid droplets (LDs) are essential for cellular lipid homeostasis by storing diverse neutral lipids (NLs), such as triacylglycerol (TAG), steryl esters (SE), and retinyl esters (RE). A proper assembly of TAG-containing LDs at the ER requires Seipin, a conserved protein often mutated in lipodystrophies. Here, we show that the yeast Seipin Sei1 and its partner Ldb16 also promote the storage of other NL in LDs. Importantly, this role of Sei1/Ldb16 is evolutionarily conserved as expression of human-Seipin restored normal SE-containing LDs in yeast Seipin mutants. As in the case of TAG, the formation of SE-containing LDs requires interactions between hydroxyl-residues in human Seipin or yeast Ldb16 with NL carboxyl esters. These findings provide a universal mechanism for Seipin-mediated LD formation and suggest a model for how Seipin distinguishes NLs from aliphatic phospholipid acyl chains in the center of the membrane bilayer.

Indexed as

GTP-Binding Protein gamma SubunitsLipid DropletsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsEndoplasmic ReticulumEstersHumansLipid MetabolismSaccharomyces cerevisiaeTriglyceridesBSCL2 protein, humanEstersGTP-Binding Protein gamma SubunitsLDB16 protein, S cerevisiaeMitochondrial ProteinsSaccharomyces cerevisiae Proteinsseipin protein, S cerevisiaeTriglycerides

Identifiers

PMID35938957
PMCPMC9365673
OpenAlexW4297489083

What OpenQuestion holds

Textmetadata
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.