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| Item Type: | Article |
|---|---|
| Title: | Identification of TMEM206 proteins as pore of PAORAC/ASOR acid-sensitive chloride channels |
| Creators Name: | Ullrich, F., Blin, S., Lazarow, K., Daubitz, T., von Kries, J.P. and Jentsch, T.J. |
| Abstract: | Acid-sensing ion channels have important functions in physiology and pathology, but the molecular composition of acid-activated chloride channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying anion channel PAORAC/ASOR. ASOR is formed by TMEM206 proteins which display two transmembrane domains (TMs) and are expressed at the plasma membrane. Ion permeation-changing mutations along the length of TM2 and at the end of TM1 suggest that these segments line ASOR's pore. While not belonging to a gene family, TMEM206 has orthologs in probably all vertebrates. Currents from evolutionarily distant orthologs share activation by protons, a feature essential for ASOR's role in acid-induced cell death. TMEM206 defines a novel class of ion channels. Its identification will help to understand its physiological roles and the diverse ways by which anion-selective pores can be formed. |
| Keywords: | PAC, Proton-Activated, I(Cl,H), CL(-) Channel, PAORAC, Animals |
| Source: | eLife |
| ISSN: | 2050-084X |
| Publisher: | eLife Sciences Publications |
| Volume: | 8 |
| Page Range: | e49187 |
| Date: | 18 July 2019 |
| Official Publication: | https://doi.org/10.7554/eLife.49187 |
| PubMed: | View item in PubMed |
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