Binding of perilipin 3 to membranes containing diacylglycerol is mediated by conserved residues within its PAT domain

Stribny, Jiri; Schneiter, Roger

doi:10.1016/j.jbc.2023.105384

Cited by 3 publications

(1 citation statement)

References 70 publications

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“…Finally, we tested the effect of 1,2 dioleoyl-glycerol (DOG) on PLIN3 binding properties. Diacylglycerols are intermediates in LD metabolism and have been shown to promote the binding of PLIN3 to lipid bilayers (15,(37)(38)(39). To quantify the effect of DOG on PLIN3 binding to bilayers, we used the membrane environment-sensitive fluorescent probe NBD (19).…”

Section: Plin3 Binding To Ld Is Hypersensitive To Surface Tensionmentioning

confidence: 99%

Surface tension-driven sorting of human perilipins on lipid droplets

Araujo,

Bello,

Bigay

et al. 2024

Preprint

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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 dependent on tension, even with polar lipids favoring packing defects, and showed an inverse correlation between protein and phospholipid densities on LDs. In contrast, PLIN1 bound readily to LDs fully covered by phospholipids; PLIN2 showed an intermediate behavior. In human adipocytes, PLIN3/4 were found in a soluble pool and relocated to LDs upon stimulation of triglyceride synthesis, whereas PLIN1 and PLIN2 localized to pre-existing LDs, consistent with the huge 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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Section: Plin3 Binding To Ld Is Hypersensitive To Surface Tensionmentioning

confidence: 99%

Surface tension-driven sorting of human perilipins on lipid droplets

Araujo,

Bello,

Bigay

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

Lipid droplets as substrates for protein phase separation

Kamatar,

Bravo,

Yuan

et al. 2024

Biophysical Journal

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Surface tension–driven sorting of human perilipins on lipid droplets

Dias Araújo,

Bello,

Bigay

et al. 2024

Journal of Cell Biology

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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.

show abstract

Binding of perilipin 3 to membranes containing diacylglycerol is mediated by conserved residues within its PAT domain

Cited by 3 publications

References 70 publications

Surface tension-driven sorting of human perilipins on lipid droplets

Surface tension-driven sorting of human perilipins on lipid droplets

Lipid droplets as substrates for protein phase separation

Surface tension–driven sorting of human perilipins on lipid droplets

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