Evidence map›Paper›PMID 33481779›Full record

ArticlePLoS biology2021

Seipin traps triacylglycerols to facilitate their nanoscale clustering in the endoplasmic reticulum membrane.

Xavier Prasanna, Veijo T Salo, Shiqian Li, Katharina Ven, Helena Vihinen, Eija Jokitalo, Ilpo Vattulainen, Elina Ikonen

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
9.3field-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

54 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
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  12. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
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  15. Review
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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

8 authors at 1 institution in 1 country.

Xavier PrasannaDepartment of Physics, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-2270-5493
Veijo T SaloDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-6991-2142
Shiqian LiDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-1663-0704
Katharina VenDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Helena VihinenInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-3862-9237
Eija JokitaloInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID 0000-0002-4159-6934
Ilpo VattulainenDepartment of Physics, University of Helsinki, Helsinki, Finland.ORCID 0000-0001-7408-3214
Elina IkonenDepartment of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Seipin is a disk-like oligomeric endoplasmic reticulum (ER) protein important for lipid droplet (LD) biogenesis and triacylglycerol (TAG) delivery to growing LDs. Here we show through biomolecular simulations bridged to experiments that seipin can trap TAGs in the ER bilayer via the luminal hydrophobic helices of the protomers delineating the inner opening of the seipin disk. This promotes the nanoscale sequestration of TAGs at a concentration that by itself is insufficient to induce TAG clustering in a lipid membrane. We identify Ser166 in the α3 helix as a favored TAG occupancy site and show that mutating it compromises the ability of seipin complexes to sequester TAG in silico and to promote TAG transfer to LDs in cells. While the S166D-seipin mutant colocalizes poorly with promethin, the association of nascent wild-type seipin complexes with promethin is promoted by TAGs. Together, these results suggest that seipin traps TAGs via its luminal hydrophobic helices, serving as a catalyst for seeding the TAG cluster from dissolved monomers inside the seipin ring, thereby generating a favorable promethin binding interface.

Indexed as

Cells, CulturedEndoplasmic ReticulumGTP-Binding Protein gamma SubunitsHEK293 CellsHumansIntracellular MembranesLipid DropletsMembrane LipidsProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryTriglyceridesBSCL2 protein, humanGTP-Binding Protein gamma SubunitsMembrane LipidsTriglycerides

Identifiers

PMID33481779
PMCPMC7857593
OpenAlexW3125614516

What OpenQuestion holds

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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.