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SLC7A11 is an unconventional H+ transporter in lysosomes

Published:24 April 2025 DOI: 10.1016/j.cell.2025.04.004
Nan Zhou, Jingzhi Chen, Meiqin Hu, Na Wen, Weijie Cai, Ping Li, Liding Zhao, Yaping Meng, Dongdong Zhao, Xiaotong Yang, Siyu Liu, Fangqian Huang, Cheng Zhao, Xinghua Feng, Zikai Jiang, Enjun Xie, Hongxu Pan, Zhidong Cen, Xinhui Chen, Wei Luo, Haoxing Xu

Abstract

Lysosomes maintain an acidic pH of 4.5–5.0, optimal for macromolecular degradation. Whereas proton influx is produced by a V-type H+ ATPase, proton efflux is mediated by a fast H+ leak through TMEM175 channels, as well as an unidentified slow pathway. A candidate screen on an orphan lysosome membrane protein (OLMP) library enabled us to discover that SLC7A11, the protein target of the ferroptosis-inducing compound erastin, mediates a slow lysosomal H+ leak through downward flux of cystine and glutamate, two H+ equivalents with uniquely large but opposite concentration gradients across lysosomal membranes. SLC7A11 deficiency or inhibition caused lysosomal over-acidification, reduced degradation, accumulation of storage materials, and ferroptosis, as well as facilitated α-synuclein aggregation in neurons. Correction of abnormal lysosomal acidity restored lysosome homeostasis and prevented ferroptosis. These studies have revealed an unconventional H+ transport conduit that is integral to lysosomal flux of protonatable metabolites to regulate lysosome function, ferroptosis, and Parkinson’s disease (PD) pathology.

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