Evidence map›Paper›PMID 32349126›Full record

ArticleThe Journal of cell biology2020

Seipin and Nem1 establish discrete ER subdomains to initiate yeast lipid droplet biogenesis.

Vineet Choudhary, Ola El Atab, Giulia Mizzon, William A Prinz, Roger Schneiter

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

59 citing papers in PubMed, 103 citations in OpenAlex.

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  11. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Vineet ChoudharyDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Ola El AtabDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
Giulia MizzonElectron Microscopy Core Facility, European Molecular Biology Laboratory, Heidelberg, Germany.
William A PrinzNational Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD.
Roger SchneiterDepartment of Biology, University of Fribourg, Fribourg, Switzerland.
University of Fribourg · CHEuropean Molecular Biology Laboratory · DENational Institutes of Health · US

Funding

Intracellular Lipid Trafficking and Organelle BiogenesisZIADK060004 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI PRINZ, WILLIAM · 2009 to 2022
$8.5M
Swiss National Science Foundation 173003
6 · The paper itself

Abstract

Lipid droplets (LDs) are fat storage organelles that originate from the endoplasmic reticulum (ER). Relatively little is known about how sites of LD formation are selected and which proteins/lipids are necessary for the process. Here, we show that LDs induced by the yeast triacylglycerol (TAG)-synthases Lro1 and Dga1 are formed at discrete ER subdomains defined by seipin (Fld1), and a regulator of diacylglycerol (DAG) production, Nem1. Fld1 and Nem1 colocalize to ER-LD contact sites. We find that Fld1 and Nem1 localize to ER subdomains independently of each other and of LDs, but both are required for the subdomains to recruit the TAG-synthases and additional LD biogenesis factors: Yft2, Pex30, Pet10, and Erg6. These subdomains become enriched in DAG. We conclude that Fld1 and Nem1 are both necessary to recruit proteins to ER subdomains where LD biogenesis occurs.

Indexed as

Diacylglycerol O-AcyltransferaseDiglyceridesEndoplasmic ReticulumGene Expression Regulation, FungalGenes, ReporterGreen Fluorescent ProteinsLipid DropletsLipid MetabolismLuminescent ProteinsMembrane ProteinsMethyltransferasesNuclear ProteinsOrganelle BiogenesisRed Fluorescent ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsdelta 24-sterol methyltransferaseDGA1 protein, S cerevisiaeDiacylglycerol O-AcyltransferaseDiglyceridesFld1 protein, S cerevisiaeGreen Fluorescent ProteinsLuminescent ProteinsMembrane ProteinsMethyltransferasesNem1 protein, S cerevisiaeNuclear ProteinsPex30 protein, S cerevisiaeRed Fluorescent ProteinSaccharomyces cerevisiae ProteinsTriglycerides

Identifiers

PMID32349126
PMCPMC7337503
OpenAlexW3019317568

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.