ArticleJournal of lipid research2016
Insertion of perilipin 3 into a glycero(phospho)lipid monolayer depends on lipid headgroup and acyl chain species.
Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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.
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Who cites it
12 citing papers in PubMed.
- A conserved sequence insert of fibrillins is involved in plastoglobule association and lipid binding.Plant & cell physiology · 2026Article
- Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation.Nature communications · 2023Article
- Changing the phospholipid composition of lipid droplets alters localization of select lipid droplet proteins.microPublication biology · 2023Article
- Perilipins at a glance.Journal of cell science · 2022Article
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- The C-Terminus of Perilipin 3 Shows Distinct Lipid Binding at Phospholipid-Oil-Aqueous Interfaces.Membranes · 2021Article
- Acylcarnitines at the Membrane Surface: Insertion Parameters for a Mitochondrial Leaflet Model.Biophysical journal · 2020Article
- A giant amphipathic helix from a perilipin that is adapted for coating lipid droplets.Nature communications · 2018Article
- Lipid bilayer composition modulates the unfolding free energy of a knotted α-helical membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes.Scientific reports · 2017Article
- The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipid droplets (LDs) are organelles that contribute to various cellular functions that are vital for life. Aside from acting as a neutral lipid storage depot, they are also involved in building new membranes, synthesis of steroid hormones, and cell signaling. Many aspects of LD structure and function are not yet well-understood. Here we investigate the interaction of perilipin 3, a member of the perilipin family of LD binding proteins, and three N-terminal truncation mutants with lipid monolayers. The interaction is studied as a function of surface pressure for a series of systematically chosen lipids. We find that the C terminus of perilipin 3 has different insertion behavior from that of the longer truncation mutants and the full-length protein. Inclusion of N-terminal sequences with the C terminus decreases the ability of the protein construct to insert in lipid monolayers. Coupling of anionic lipids to negative spontaneous curvature facilitates protein interaction and insertion. The C terminus shows strong preference for lipids with more saturated fatty acids. This work sheds light on the LD binding properties and function of the different domains of perilipin 3.
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Registered trials
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