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Identification of TMEM206 proteins as pore of ASOR acid-sensitive chloride channels

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Item Type:Preprint
Title:Identification of TMEM206 proteins as pore of ASOR acid-sensitive chloride channels
Creators Name:Ullrich, F. and Blin, S. and Lazarow, K. and Daubitz, T. and 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 anion channels had remained unclear. We now used a genome-wide siRNA screen to molecularly identify the widely expressed acid-sensitive outwardly-rectifying ASOR chloride channel. 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:PAORAC, PAC, Proton-Activated, I(Cl,H), Cl(-) Channel
Publisher:Cold Spring Harbor Laboratory Press
Article Number:667600
Date:11 June 2019
Official Publication:https://doi.org/10.1101/667600
Related to:
https://edoc.mdc-berlin.de/18337/Final version

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