Evidence map›Paper›PMID 35210614›Full record

ArticleNature structural & molecular biology2022

Seipin forms a flexible cage at lipid droplet formation sites.

Henning Arlt, Xuewu Sui, Brayden Folger, Carson Adams, Xiao Chen, Roman Remme, Fred A Hamprecht, Frank DiMaio, Maofu Liao, Joel M Goodman and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
12.4field-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

58 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Heterogeneity, dynamics and organelle interactions of lipid droplets.Nature reviews. Molecular cell biology · 2026
    Review
  6. Polyunsaturated fatty acid metabolism in the retinal pigment epithelium and its association with outer retinal disease.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Review
  7. Article
  8. Review
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  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Loss of Nuclear TDP-43 Impairs Lipid Metabolism in Microglia-Like Cells.bioRxiv : the preprint server for biology · 2025
    Article
  20. Article
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

12 authors at 7 institutions in 2 countries.

Henning ArltDepartment of Molecular Metabolism, Harvard T. H. Chan School of Public Health, Boston, MA, USA.ORCID http://orcid.org/0000-0001-6395-9620
Xuewu SuiDepartment of Molecular Metabolism, Harvard T. H. Chan School of Public Health, Boston, MA, USA.
Brayden FolgerDepartment of Pharmacology, University of Texas Southwestern Medical School, Dallas, TX, USA.
Carson AdamsDepartment of Biochemistry and Institute of Protein Design, University of Washington, Seattle, WA, USA.
Xiao ChenDepartment of Pharmacology, University of Texas Southwestern Medical School, Dallas, TX, USA.
Roman RemmeHeidelberg Collaborative for Image Processing, Interdisciplinary Center for Scientific Computing, Heidelberg University, Heidelberg, Germany.
Fred A HamprechtHeidelberg Collaborative for Image Processing, Interdisciplinary Center for Scientific Computing, Heidelberg University, Heidelberg, Germany.
Frank DiMaioDepartment of Biochemistry and Institute of Protein Design, University of Washington, Seattle, WA, USA.
Maofu LiaoDepartment of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-3481-450X
Joel M Goodman *Department of Pharmacology, University of Texas Southwestern Medical School, Dallas, TX, USA. Joel.Goodman@UTSouthwestern.edu.
Robert V Farese *Department of Molecular Metabolism, Harvard T. H. Chan School of Public Health, Boston, MA, USA. robert@hsph.harvard.edu.ORCID http://orcid.org/0000-0001-8103-2239
Tobias C Walther *Department of Molecular Metabolism, Harvard T. H. Chan School of Public Health, Boston, MA, USA. twalther@hsph.harvard.edu.ORCID http://orcid.org/0000-0003-1442-1327
Broad Institute · USHarvard University · USHeidelberg University · DEThe University of Texas Southwestern Medical Center · USUniversity of Washington · USHoward Hughes Medical Institute · USSouthwestern Medical Center · US

Funding

A Simple Cellular Model for LipodystrophyR01GM084210 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI GOODMAN, JOEL M · 2008 to 2021
$4.0M
Mechanisms of Lipid Droplet FormationR01GM124348 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI FARESE, ROBERT V · 2017 to 2024
$2.9M
Protein structure determination from low-resolution experimental dataR01GM123089 · NIGMS · UNIVERSITY OF WASHINGTON · PI DIMAIO, FRANK P · 2017 to 2025
$2.6M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM084210NIGMS NIH HHS R01 GM123089NIGMS NIH HHS R01 GM124348
6 · The paper itself

Abstract

Lipid droplets (LDs) form in the endoplasmic reticulum by phase separation of neutral lipids. This process is facilitated by the seipin protein complex, which consists of a ring of seipin monomers, with a yet unclear function. Here, we report a structure of S. cerevisiae seipin based on cryogenic-electron microscopy and structural modeling data. Seipin forms a decameric, cage-like structure with the lumenal domains forming a stable ring at the cage floor and transmembrane segments forming the cage sides and top. The transmembrane segments interact with adjacent monomers in two distinct, alternating conformations. These conformations result from changes in switch regions, located between the lumenal domains and the transmembrane segments, that are required for seipin function. Our data indicate a model for LD formation in which a closed seipin cage enables triacylglycerol phase separation and subsequently switches to an open conformation to allow LD growth and budding.

Indexed as

GTP-Binding Protein gamma SubunitsLipid DropletsEndoplasmic ReticulumLipid MetabolismMembrane ProteinsSaccharomyces cerevisiaeGTP-Binding Protein gamma SubunitsMembrane Proteins

Identifiers

PMID35210614
PMCPMC8930772
OpenAlexW4220940324

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.