Evidence map›Paper›PMID 26572621›Full record

ArticleThe Journal of cell biology2015

The seipin complex Fld1/Ldb16 stabilizes ER-lipid droplet contact sites.

Alexandra Grippa, Laura Buxó, Gabriel Mora, Charlotta Funaya, Fatima-Zahra Idrissi, Francesco Mancuso, Raul Gomez, Júlia Muntanyà, Eduard Sabidó, Pedro Carvalho

Abstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

114 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. Article
  6. Article
  7. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
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  18. Review
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  20. Article

54 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

10 authors.

Alexandra GrippaCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Laura BuxóCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Gabriel MoraCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Charlotta FunayaElectron Microscopy Core Facility, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Fatima-Zahra IdrissiCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Francesco MancusoCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Raul GomezCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Júlia MuntanyàCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain.
Eduard SabidóCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Pedro CarvalhoCentre for Genomic Regulation, The Barcelona Institute of Science and Technology, 08003 Barcelona, Spain Universitat Pompeu Fabra, 08003 Barcelona, Spain pedro.carvalho@crg.eu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid droplets (LDs) are storage organelles consisting of a neutral lipid core surrounded by a phospholipid monolayer and a set of LD-specific proteins. Most LD components are synthesized in the endoplasmic reticulum (ER), an organelle that is often physically connected with LDs. How LD identity is established while maintaining biochemical and physical connections with the ER is not known. Here, we show that the yeast seipin Fld1, in complex with the ER membrane protein Ldb16, prevents equilibration of ER and LD surface components by stabilizing the contact sites between the two organelles. In the absence of the Fld1/Ldb16 complex, assembly of LDs results in phospholipid packing defects leading to aberrant distribution of lipid-binding proteins and abnormal LDs. We propose that the Fld1/Ldb16 complex facilitates the establishment of LD identity by acting as a diffusion barrier at the ER-LD contact sites.

Indexed as

Cell MembraneEndoplasmic ReticulumGTP-Binding Protein gamma SubunitsLipid DropletsMembrane ProteinsMitochondrial ProteinsPhospholipidsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFld1 protein, S cerevisiaeGTP-Binding Protein gamma SubunitsLDB16 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsPhospholipidsSaccharomyces cerevisiae Proteinsseipin protein, S cerevisiae

Identifiers

PMID26572621
PMCPMC4657162

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.