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SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis

ABSTRACT: This study investigates how loss of the ER transporter SLC33A1 affects glutathione redox balance and protein cysteine reactivity in the endoplasmic reticulum. Oxidized cysteine reactivity profiling and whole-cell proteomics were performed in Slc33a1 knockout KPK cells and cDNA-complemented controls. Quantitative TMT-based proteomics identified increased oxidation of protein disulfide isomerases and other ER-resident proteins, indicating disruption of ER redox homeostasis and proteostasis. Additional experiments examined unfolded protein response activation and genetic interactions with ER quality-control pathways. The dataset includes cysteine reactivity profiling and unenriched proteomics data acquired by LC–MS/MS and processed using standard proteomics pipelines.

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Lung Cancer

SUBMITTER: Shanshan Liu

LAB HEAD: Kivanc, Birsoy

PROVIDER: PXD074382 | Pride | 2026-02-13

REPOSITORIES: Pride

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			Action	DRS
	KPK_oxidized_cysteine_reactivity.xlsx	Xlsx
	MS238381ASC_Shanshan_Birsoy_Complete_original.xlsx	Xlsx
	checksum.txt	Txt

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