Evolutionarily conserved roles of Caenorhabditis elegans perilipin in lipolysis
- Published
- Accepted
- Subject Areas
- Cell Biology, Evolutionary Studies, Molecular Biology
- Keywords
- Perilipin, PLIN-1, Lipid metabolism, Lipolysis, Caenorhabditis elegans, ATGL, HSL, Lipophagy, Lipid droplets, Autophagy
- Copyright
- © 2019 Kaššák et al.
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ Preprints) and either DOI or URL of the article must be cited.
- Cite this article
- 2019. Evolutionarily conserved roles of Caenorhabditis elegans perilipin in lipolysis. PeerJ Preprints 7:e27467v1 https://doi.org/10.7287/peerj.preprints.27467v1
Abstract
Neutral lipids and namely triacyl-glycerols (TAGs) are the prevalent excess energy storage molecules in all eukaryotic organisms. They are universally organized in active cytoplasmic organelles called lipid droplets (LDs) and their breakdown is performed and regulated in an evolutionarily conserved manner. In mammals, two distinct but inter-connected pathways are believed to mediate this catabolism: conventional cytoplasmic lipolysis with effector neutral lipases; and lipophagy, a specific kind of autophagy exploiting lysosomal acidic lipases. Central molecules in this regulation are LD-resident proteins, perilipins (PLINs). Our recent discovery of a sole PLIN orthologue in C. elegans offers a unique opportunity to study these regulatory pathways, provided that the interactive mechanisms are orthologous. To determine this, we employed classical genetics with genome editing tools and in vivo microscopy to provide three lines of evidence demonstrating the conserved role of the C. elegans perilipin. Firstly, we proved the common presence of a standard lipolytic apparatus on LDs. Next, we ascertained a functional connection between nematode PLIN-1 and the effector enzyme, hormone-sensitive lipase (HOSL-1). Finally, we identified lipophagy as a secondary lipolytic pathway, which is consistent with the mammalian model. Our data provide not only a proof of concept but also suggests interesting implications by questioning the physiological role of lipophagy in lipolysis.
Author Comment
This is a submission to PeerJ for review.
Supplemental Information
Cloning strategy overview for the construction of a rescue plasmid used in CAS9/CRISPR-dependent mKate2 insertion next to the native locus of PLIN-1
Raw data of experiments represented in Fig. 3-5
(Sheet 1) Animal counting in the experiment represented in Fig. 3. (Sheet 2) Animal counting in the experiments represented in Fig. 5. (Sheet 3) Object analysis in the images, represented in Fig. 4.
Raw images used in object analysis represented in Fig. 4
(Supplementary Figure S4-S6) Individual analysed 8-bit TIFF 5µm z-stack images cropped to the analysed extent of the first embryos in the control line RD204. (Supplementary Figure S7-S9) Individual analysed 8-bit TIFF 5µm z-stack images cropped to the analysed extent of the first embryos in the experimental line KV2.