Human OTOP3 requires strong acidification for activation and exhibits mixed proton-anion permeation
Tiago D.C. Morais, Fatemeh M. Badizi, Itai Itzhak, Moushumi A. Mou, Justin Chan, Anonnya Debi, Zhifei Wang, Yong Yu · 2026
Read Human OTOP3 requires strong acidification for activation and exhibits mixed proton-anion permeation by Tiago D.C. Morais, Fatemeh M. Badizi, Itai Itzhak, Moushumi A. Mou, Justin Chan, Anonnya Debi, Zhifei Wang, Yong Yu (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-13579931.txt.
Description
Morais and co-authors present a 2026 cell physiology study of a human proton channel called OTOP3. Channels in this family let protons cross cell membranes; one sibling serves as the sour taste sensor, but OTOP3's job is unclear. Working with frog eggs fitted with the human channel, the team probed how it switches on.
The human channel needed much stronger acid to open than its mouse counterpart, a difference traced to one exposed loop of the protein. Under strong acid it also did something its siblings never do: it let negative ions slip through alongside protons, and the two currents rose and fell together under mutations. The authors suggest OTOP3 is built for very acidic niches in the body.
Catalog record
| CREATOR | Tiago D.C. Morais, Fatemeh M. Badizi, Itai Itzhak, Moushumi A. Mou, Justin Chan, Anonnya Debi, Zhifei Wang, Yong Yu |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 48 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |