AI Article Synopsis
- This research focuses on how specific proteins accumulate on lipid droplets (LDs) from the endoplasmic reticulum (ER), particularly exploring the roles of hydrophobic membrane motifs in this process.
- The study identifies vital factors, such as tryptophans and positively charged residues, that influence the proteins GPAT4 and ALG14's targeting to LDs.
- The findings suggest a unique combination of sequence features that differentiate LD-targeting proteins from those that do not accumulate on lipid droplets.
Article Abstract
Lipid droplet (LD) formation from the endoplasmic reticulum (ER) is accompanied by the targeting and accumulation of specific hydrophobic, membrane-embedded proteins on LDs. The determinants of this process are unknown. Here, we study the hydrophobic membrane motifs of two Drosophila melanogaster proteins, GPAT4 and ALG14, that utilize this pathway, and we identify crucial sequence features that mediate LD accumulation. Molecular dynamics simulations and studies in cells reveal that LD targeting of these motifs requires deeply inserted tryptophans that have lower free energy in the LD oil phase and positively charged residues near predicted hairpin hinges that become less constrained in the LD environment. Analyzing hydrophobic motifs from similar LD-targeting proteins, it appears that the distribution of tryptophan and positively charged residues distinguishes them from non-LD-targeting membrane motifs. Our studies identify specific sequence features and principles of hydrophobic membrane motifs that mediate their accumulation on LDs.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7696655 | PMC |
| http://dx.doi.org/10.1016/j.devcel.2020.07.001 | DOI Listing |
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