Evidence map›Paper›PMID 31708432›Full record

ArticleDevelopmental cell2019

LDAF1 and Seipin Form a Lipid Droplet Assembly Complex.

Jeeyun Chung, Xudong Wu, Talley J Lambert, Zon Weng Lai, Tobias C Walther, Robert V Farese

Open access · greenAbstract read
In one paragraph

Article in Developmental cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
16.2field-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

134 citing papers in PubMed, 226 citations in OpenAlex.

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  10. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
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  19. Lipid Droplet Dynamics in Alcoholic Steatohepatitis.The American journal of pathology · 2026
    Review
  20. Article

74 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Jeeyun ChungDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA.
Xudong WuDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Talley J LambertDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Zon Weng LaiDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Harvard Chan Advanced Multi-omics Platform, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA.
Tobias C WaltherDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Harvard Chan Advanced Multi-omics Platform, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Broad Institute of Harvard and MIT, Cambridge, MA 02124, USA; Howard Hughes Medical Institute, Boston, MA 02115, USA. Electronic address: twalther@hsph.harvard.edu.
Robert V FareseDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Boston, MA 02115, USA; Broad Institute of Harvard and MIT, Cambridge, MA 02124, USA. Electronic address: robert@hsph.harvard.edu.
Harvard University · USBroad Institute · USCenter for Systems Biology · US

Funding

Mechanisms of Lipid Droplet Protein TargetingR01GM097194 · NIGMS · YALE UNIVERSITY · PI WALTHER, TOBIAS C · 2011 to 2024
$4.9M
Mechanisms of Lipid Droplet FormationR01GM124348 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI FARESE, ROBERT V · 2017 to 2024
$2.9M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM097194NIGMS NIH HHS R01 GM124348
6 · The paper itself

Abstract

Lipid droplets (LDs) originate from the endoplasmic reticulum (ER) to store triacylglycerol (TG) and cholesterol esters. The ER protein seipin was shown to localize to ER-LD contacts soon after LDs form, but what determines the sites of initial LD biogenesis in the ER is unknown. Here, we identify TMEM159, now re-named lipid droplet assembly factor 1 (LDAF1), as an interaction partner of seipin. Together, LDAF1 and seipin form an ∼600 kDa oligomeric complex that copurifies with TG. LDs form at LDAF1-seipin complexes, and re-localization of LDAF1 to the plasma membrane co-recruits seipin and redirects LD formation to these sites. Once LDs form, LDAF1 dissociates from seipin and moves to the LD surface. In the absence of LDAF1, LDs form only at significantly higher cellular TG concentrations. Our data suggest that the LDAF1-seipin complex is the core protein machinery that facilitates LD biogenesis and determines the sites of their formation in the ER.

Indexed as

Cell Line, TumorEndoplasmic ReticulumGTP-Binding Protein gamma SubunitsHEK293 CellsHumansLipid DropletsMembrane ProteinsProtein BindingTriglyceridesBSCL2 protein, humanGTP-Binding Protein gamma SubunitsMembrane ProteinsTMEM159 protein, humanTriglyceridesBerardinelli-Seip congenital lipodystrophy type 2endoplasmic reticulumfatlipid dropletslipodystrophyorganelle biogenesispromethinTMEM159triacylglycerol

Identifiers

PMID31708432
PMCPMC7235935
OpenAlexW2988365714

What OpenQuestion holds

Textmetadata
LicenceTDM
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.