TMEM16 and TMEM63/OSCA proteins share a conserved potential to permeate ions and phospholipids

Author:

Lowry Augustus J.1,Liang Pengfei1,Serena Wan Y.C.1,Pei Zhen-Ming2,Yang Huanghe13ORCID,Zhang Yang1

Affiliation:

1. Department of Biochemistry, Duke University School of Medicine

2. Department of Biology, Duke University

3. Department of Neurobiology, Duke University School of Medicine

Abstract

The calcium-activated TMEM16 proteins and the mechanosensitive/osmolarity-activated OSCA/TMEM63 proteins belong to the Transmembrane Channel/Scramblase (TCS) superfamily. Within the superfamily, OSCA/TMEM63 proteins, as well as TMEM16A and TMEM16B, likely function solely as ion channels. However, the remaining TMEM16 members, including TMEM16F, maintain an additional function as scramblases, rapidly exchanging phospholipids between leaflets of the membrane. Although recent studies have advanced our understanding of TCS structure-function relationships, the molecular determinants of TCS ion and lipid permeation remain unclear. Here we show that single lysine mutations in transmembrane helix (TM) 4 allow non-scrambling TCS members to permeate phospholipids. This study highlights the key role of TM 4 in controlling TCS ion and lipid permeation and offers novel insights into the evolution of the TCS superfamily, suggesting that, like TMEM16s, the OSCA/TMEM63 family maintains a conserved potential to permeate ions and phospholipids.

Publisher

eLife Sciences Publications, Ltd

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