Evidence map›Paper›PMID 35583926›Full record

ArticleeLife2022

Seipin transmembrane segments critically function in triglyceride nucleation and lipid droplet budding from the membrane.

Siyoung Kim, Jeeyun Chung, Henning Arlt, Alexander J Pak, Robert V Farese, Tobias C Walther, Gregory A Voth

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
7.8field-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

30 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Mechanism for oil-phase separation by the lipid droplet assembly complex.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Essential Biology of Lipid Droplets.Annual review of biochemistry · 2025
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Making the cut: Multiscale simulation of membrane remodeling.Current opinion in structural biology · 2024
    Review
  18. Article
  19. Review
  20. 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

7 authors at 5 institutions in 1 country.

Siyoung KimPritzker School of Molecular Engineering, University of Chicago, Chicago, United States.ORCID 0000-0003-4670-9747
Jeeyun ChungDepartment of Molecular Metabolism, Harvard T H Chan School of Public Health, Boston, United States.ORCID 0000-0002-4617-7181
Henning ArltDepartment of Molecular Metabolism, Harvard T H Chan School of Public Health, Boston, United States.
Alexander J PakDepartment of Chemical and Biological Engineering, Colorado School of Mines, Golden, United States.
Robert V FareseDepartment of Molecular Metabolism, Harvard T H Chan School of Public Health, Boston, United States.ORCID 0000-0001-8103-2239
Tobias C WaltherDepartment of Molecular Metabolism, Harvard T H Chan School of Public Health, Boston, United States.
Gregory A VothDepartment of Chemistry, Chicago Center for Theoretical Chemistry, James Franck Institute, and Institute for Biophysical Dynamics, The University of Chicago, Chicago, United States.ORCID 0000-0002-3267-6748
Boston University · USBroad Institute · USChicago Institute for Psychoanalysis · USColorado School of Mines · USUniversity of Chicago · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
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
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM063796NIGMS NIH HHS R01 GM097194NIGMS NIH HHS R01 GM124348
6 · The paper itself

Abstract

Lipid droplets (LDs) are organelles formed in the endoplasmic reticulum (ER) to store triacylglycerol (TG) and sterol esters. The ER protein seipin is key for LD biogenesis. Seipin forms a cage-like structure, with each seipin monomer containing a conserved hydrophobic helix and two transmembrane (TM) segments. How the different parts of seipin function in TG nucleation and LD budding is poorly understood. Here, we utilized molecular dynamics simulations of human seipin, along with cell-based experiments, to study seipin's functions in protein-lipid interactions, lipid diffusion, and LD maturation. An all-atom simulation indicates that seipin TM segment residues and hydrophobic helices residues located in the phospholipid tail region of the bilayer attract TG. Simulating larger, growing LDs with coarse-grained models, we find that the seipin TM segments form a constricted neck structure to facilitate conversion of a flat oil lens into a budding LD. Using cell experiments and simulations, we also show that conserved, positively charged residues at the end of seipin's TM segments affect LD maturation. We propose a model in which seipin TM segments critically function in TG nucleation and LD growth.

Indexed as

Endoplasmic ReticulumLipid DropletsHumansMembranesPhospholipidsTriglyceridesPhospholipidsTriglycerideshumanlipid dropletsmolecular biophysicsmolecular dynamicsseipinstructural biology

Identifiers

PMID35583926
PMCPMC9122495
OpenAlexW4280626133

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.