Surface tension–driven sorting of human perilipins on lipid droplets - Archive ouverte HAL
Article Dans Une Revue Journal of Cell Biology Année : 2024

Surface tension–driven sorting of human perilipins on lipid droplets

Ana Rita Dias Araújo
Abdoul Akim Bello
Céline Franckhauser
Romain Gautier
Julie Cazareth
Dávid Kovács
Frédéric Brau
Nicolas Fuggetta
Alenka Čopič
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Résumé

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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Dates et versions

hal-04779919 , version 1 (13-11-2024)

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Ana Rita Dias Araújo, Abdoul Akim Bello, Joëlle Bigay, Céline Franckhauser, Romain Gautier, et al.. Surface tension–driven sorting of human perilipins on lipid droplets. Journal of Cell Biology, 2024, 223 (12), ⟨10.1083/jcb.202403064⟩. ⟨hal-04779919⟩
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