Cited by 21Lipid metabolism and biosynthesisLipid metabolism and disordersLipid Membrane Structure and Behavior

Surface tension–driven sorting of human perilipins on lipid droplets

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Dias Araújo, Ana Rita, Bello, Abdoul Akim, Bigay, Joëlle, Franckhauser, Céline, Gautier, Romain, Cazareth, Julie, Kovács, Dávid, Brau, Frédéric +3 more·2024·Journal of Cell Biology

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Abstract

Perilipins (PLINs), the most abundant proteins on lipid droplets (LDs), display similar domain organization including amphipathic helices (AH). However, the five human PLINs bind different LDs, suggesting different modes of interaction. We established a minimal system whereby artificial LDs covered with defined polar lipids were transiently deformed to promote surface tension. Binding of purified PLIN3 and PLIN4 AH was strongly facilitated by tension but was poorly sensitive to phospholipid composition and to the presence of diacylglycerol. Accordingly, LD coverage by PLIN3 increased as phospholipid coverage decreased. In contrast, PLIN1 bound readily to LDs fully covered by phospholipids; PLIN2 showed an intermediate behavior between PLIN1 and PLIN3. In human adipocytes, PLIN3/4 were found in a soluble pool and relocated to LDs upon stimulation of fast triglyceride synthesis, whereas PLIN1 and PLIN2 localized to pre-existing LDs, consistent with the large difference in LD avidity observed in vitro. We conclude that the PLIN repertoire is adapted to handling LDs with different surface properties.

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  • Lipid droplets with higher levels of unsaturation exhibit packing defects and increased protein binding.

    “Several biophysical studies have reported that lipid droplets with higher levels of unsaturation exhibit packing defects and increased protein binding55,56.”

    From APOE genotypes differentially remodel the astrocytic lipid droplet proteome to shape lipid droplet dynamics (2026) · cites this paper as [56]

    The Results section on LD packing defects reports that greater PC unsaturation increased defects at high phospholipid coverage (low tension). The Results also report increased binding to more-unsaturated artificial lipid droplets for PLIN2 and a smaller increase for PLIN3. The claim omits these conditions: at higher tension, shallow defects increased regardless of PC unsaturation, so the paper does not support the relationship as a general property of lipid droplets. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
Dias Araújo, A. R., Bello, A. A., Bigay, J., Franckhauser, C., Gautier, R., Cazareth, J., Kovács, D., Brau, F., Fuggetta, N., Čopič, A., & Antonny, B.
Affiliations
  • Université Côte d’Azur, CNRS and Inserm, Institut de Pharmacologie Moléculaire et Cellulaire, UMR 7275 1 , Sophia Antipolis, France
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Bigay, Joëlle
  • Čopič, Alenka
  • Antonny, Bruno
Venue
Journal of Cell Biology
Published
2024-09-19
Volume
223
Issue
12
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W4402642777
Cited by
21
References
1
Citations by year
2026: 11 · 2025: 10
FWCI
3.23
Type
journal article
Language
en
Open access
Locations
  • The Journal of Cell Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
Funders
  • European Research Council (856404)
  • Agence Nationale de la Recherche (ANR-10-INBS-04, ANR-15-IDEX-01)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords
perilipin, lipid droplets, surface tension, amphipathic helix, PLIN3, PLIN4, PLIN1, PLIN2, phospholipid composition, diacylglycerol, adipocytes, triglyceride synthesis, protein sorting
MeSH terms
Perilipins, Perilipin-1, Perilipin-2, Perilipin-3, Perilipin-4, Humans, Phospholipids, Protein Binding, Surface Tension, Triglycerides, Adipocytes, Protein Transport, Lipid Droplets

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