Evidence map›Paper›PMID 30901948›Full record

ArticleCells2019

Promethin Is a Conserved Seipin Partner Protein.

Inês G Castro, Michal Eisenberg-Bord, Elisa Persiani, Justin J Rochford, Maya Schuldiner, Maria Bohnert

Open access · goldAbstract read
In one paragraph

Article in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 76 citations in OpenAlex.

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

6 authors at 3 institutions in 3 countries.

Inês G CastroDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. ines.castro@weizmann.ac.il.
Michal Eisenberg-BordDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. michal.eisenberg@weizmann.ac.il.
Elisa PersianiRowett Institute and Aberdeen Cardiovascular and Diabetes Centre, University of Aberdeen, Aberdeen, AB25 2ZD, UK. e.persiani@abdn.ac.uk.
Justin J RochfordRowett Institute and Aberdeen Cardiovascular and Diabetes Centre, University of Aberdeen, Aberdeen, AB25 2ZD, UK. j.rochford@abdn.ac.uk.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. maya.schuldiner@weizmann.ac.il.
Maria BohnertDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel. bohnertm@uni-muenster.de.
Weizmann Institute of Science · ILUniversity of Aberdeen · GBUniversity of Münster · DE

Funding

Biotechnology and Biological Sciences Research Council BB/K017772/1Medical Research Council MR/L002620/1
6 · The paper itself

Abstract

Seipin (BSCL2/SPG17) is a key factor in lipid droplet (LD) biology, and its dysfunction results in severe pathologies, including the fat storage disease Berardinelli-Seip congenital lipodystrophy type 2, as well as several neurological seipinopathies. Despite its importance for human health, the molecular role of seipin is still enigmatic. Seipin is evolutionarily conserved from yeast to humans. In yeast, seipin was recently found to cooperate with the lipid droplet organization (LDO) proteins, Ldo16 and Ldo45, two structurally-related proteins involved in LD function and identity that display remote homology to the human protein promethin/TMEM159. In this study, we show that promethin is indeed an LD-associated protein that forms a complex with seipin, and its localization to the LD surface can be modulated by seipin expression levels. We thus identify promethin as a novel seipin partner protein.

Indexed as

Conserved SequenceAdipogenesisGTP-Binding Protein gamma SubunitsHEK293 CellsHumansLipid DropletsMCF-7 CellsProteinsUp-RegulationBSCL2 protein, humanGTP-Binding Protein gamma SubunitsProteinsadipogenesisBSCL2LDLDOlipid dropletlipodystrophypromethinseipinSPG17TMEM159

Identifiers

PMID30901948
PMCPMC6468817
OpenAlexW2922602727

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.