Lipid traffic: an enigmatic alliance between ORPs and a TMEM16-like protein at membrane contact sites
Alicia Fabbre, Guillaume Drin · 2026
Read Lipid traffic: an enigmatic alliance between ORPs and a TMEM16-like protein at membrane contact sites by Alicia Fabbre, Guillaume Drin (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/pmc-13286939.txt.
Description
Alicia Fabbre and Guillaume Drin review a yeast system that moves a key membrane fat from its birthplace to the cell surface. Their 2026 article explains that the fat, phosphatidylserine, is made in the endoplasmic reticulum yet piles up in the plasma membrane, where it helps recruit signaling proteins. Two transfer proteins, Osh6 and Osh7, shuttle it across the gap where the two membranes nearly touch.
A partner protein, Ist2, anchors the shuttles at that contact site through a long floppy tether, much longer than the gap itself, which raises puzzles about how transfer works. Ist2 can also flip fats across its own membrane. Whether that flipping powers the exchange remains unknown. The system, the authors argue, is a model for coordinating transport at membrane junctions.
Catalog record
| CREATOR | Alicia Fabbre, Guillaume Drin |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 33 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |