Phosphatidylethanolamine binds to human perilipins via a hydrophobic cleft in their 4-helix bundle domain for lipid droplet targeting
Jiri Stribny, Roger Schneiter · 2026
Read Phosphatidylethanolamine binds to human perilipins via a hydrophobic cleft in their 4-helix bundle domain for lipid droplet targeting by Jiri Stribny, Roger Schneiter (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13382019.txt.
Description
Jiri Stribny and Roger Schneiter report a 2026 study on how perilipin proteins find and coat fat droplets inside cells. These proteins control how stored fat is built up and broken down. Each has a bundle of four helices at one end whose fat-sensing role was unknown.
The team shows that the bundle contains a greasy groove that specifically binds one membrane fat, called PE in the work, which helps membranes bend as droplets form. Particles rich in that fat attracted the bundle strongly, while changes that closed the groove blocked binding. In yeast cells, lowering that fat reduced perilipin at droplets. The binding ability is shared across several family members.
Catalog record
| CREATOR | Jiri Stribny, Roger Schneiter |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 65680 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |