Lipid transfer proteins and PI4KIIα generate a phosphoinositide-linked proteome
Noah D. Carrillo, Mo Chen, Poorwa Awasthi, Tianmu Wen, Xiangqin Chen, Giang Vu, Dhruv Brahmbhatt, Michael Herlihy, Benjamin B. Minkoff, Michael Sussman, Vincent L. Cryns, Richard A. Anderson · 2026
Read Lipid transfer proteins and PI4KIIα generate a phosphoinositide-linked proteome by Noah D. Carrillo, Mo Chen, Poorwa Awasthi, Tianmu Wen, Xiangqin Chen, Giang Vu, Dhruv Brahmbhatt, Michael Herlihy, Benjamin B. Minkoff, Michael Sussman, Vincent L. Cryns, Richard A. Anderson (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-13266111.txt.
Description
Fat-based messengers usually work from cell membranes, but a growing list of proteins carry them as attachments in the cell's watery interior and nucleus. Noah Carrillo and co-authors map that hidden network in a 2026 study. Two lipid shuttle proteins and one lipid-making enzyme, they show, are needed to stamp the messengers onto many different proteins.
The stamped set, which they dub a new kind of proteome, clusters in metabolism, cell movement and division, and DNA damage response. The attachments survive harsh lab treatment, behaving like a true chemical modification. Stress pulls the stamping machinery into the nucleus, tying the system to the cell's alarm pathways.
Catalog record
| CREATOR | Noah D. Carrillo, Mo Chen, Poorwa Awasthi, Tianmu Wen, Xiangqin Chen, Giang Vu, Dhruv Brahmbhatt, Michael Herlihy, Benjamin B. Minkoff, Michael Sussman, Vincent L. Cryns, Richard A. Anderson |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 53 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |