Cystinosin/Ers1 functions in redox homeostasis in the early secretory pathway

gene, which encodes the highly conserved lysosomal membrane protein, cystinosin. Cystinosin mediates proton-coupled transport of cystine, the oxidized dimer of cysteine. Loss of cystinosin function leads to cystine accumulation in the lysosomal lumen. However, reduction of cystine load in the lysosomes is insufficient to treat key disease symptoms, indicating that cystinosin performs additional disease-relevant functions. Here, we report that Ers1, the yeast homolog of cystinosin, localizes to and functions in the early secretory pathway. We provide evidence that Ers1 does not transport cystine. Ers1 genetically interacts with early secretory pathway recycling adaptors and redox-active Fe-S cluster-binding proteins. Notably, cystinosin-LKG, an alternatively spliced isoform of cystinosin with altered subcellular localization beyond lysosomes, can functionally replace Ers1 in yeast. Collectively, our work uncovers a conserved role of cystinosin/Ers1 in the early secretory pathway, offering new molecular insights for understanding cystinosis pathology.

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Journal
Molecular Biology of the Cell
Published
2026-08-26
DOI
https://doi.org/10.1091/mbc.e26-03-0134
Primary Topic
Biomedical Research and Pathophysiology
Type
article
Field-Weighted Citation Impact
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article

Cystinosin/Ers1 functions in redox homeostasis in the early secretory pathway

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Molecular Biology of the Cell
Biomedical Research and Pathophysiology
article

Cystinosin/Ers1 functions in redox homeostasis in the early secretory pathway

Katie Munechika, Aleksandra Skirycz, Jade Bowerman, Richa Sardana, Haiyuan Yu, J. Zhu, Miguel Piñeros, Solomon Baik, Aleksandra Skirycz, Nathan Wu, Sumanth Mosale, Sumanth Mosale Seetharam
article en

Abstract

gene, which encodes the highly conserved lysosomal membrane protein, cystinosin. Cystinosin mediates proton-coupled transport of cystine, the oxidized dimer of cysteine. Loss of cystinosin function leads to cystine accumulation in the lysosomal lumen. However, reduction of cystine load in the lysosomes is insufficient to treat key disease symptoms, indicating that cystinosin performs additional disease-relevant functions. Here, we report that Ers1, the yeast homolog of cystinosin, localizes to and functions in the early secretory pathway. We provide evidence that Ers1 does not transport cystine. Ers1 genetically interacts with early secretory pathway recycling adaptors and redox-active Fe-S cluster-binding proteins. Notably, cystinosin-LKG, an alternatively spliced isoform of cystinosin with altered subcellular localization beyond lysosomes, can functionally replace Ers1 in yeast. Collectively, our work uncovers a conserved role of cystinosin/Ers1 in the early secretory pathway, offering new molecular insights for understanding cystinosis pathology.

Molecular Biology of the Cell
Cornell University (US), Robert W. Holley Center for Agriculture & Health (US), Michigan State University (US)
National Institute of General Medical Sciences
Good health and well-being
Openalex Percentile: Top 83%
Biomedical Research and Pathophysiology
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