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Cysteine redoxome landscape in the liver of male mice fed a high-fat high sucrose diet

ABSTRACT: Reversible cysteine post-translational modifications serve as a "switch" for protein structure-function dynamics. Herein, we established a strategy for comprehensively mapping the cysteine redoxome by pinpointing oxidized and reduced cysteine residues in the liver of male mice fed a high-fat/high-sucrose diet (HFHSD). We identified 3,151 and 2,361 labeled cysteine residues on 961 and 804 proteins in the normal chow diet and HFHSD groups, respectively. HFHSD shifts the cysteine redox states towards oxidation, especially in the mitochondria. The oxidized and reduced cysteine residues exclusively in the HFHSD group are enriched in cellular redox homeostasis, mitochondrial ATP metabolism, post-translational modifications, and disease-associated pathways. Exclusively reduced cysteine residues in the HFHSD group display a distinct consensus cysteine thiol motif, E[RK]C. The current cysteine redoxome strategy broadens the disease-associated proteome landscape and provides potential therapeutic target cysteine residues critical for regulating protein functions and interactions relevant to pathophysiology.

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Toshinari Takamura

PROVIDER: PXD053900 | JPOST Repository | Sat Jul 12 00:00:00 BST 2025

REPOSITORIES: jPOST

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			Action	DRS
	1_WT_Liver_5ACN_20220823.raw	Raw
	1_WT_Liver_Step_10_050ACN_20220712.raw	Raw
	2_WT_Liver_10ACN_20220823.raw	Raw
	2_WT_Liver_Step_10_075ACN_20220712.raw	Raw
	3_1_WT_NC_Liver_1_5ACN_20230929.raw	Raw

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