Proteomics

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A ROS-mediated Oxidation-O-GlcNAcylation cascade governs ferroptosis


ABSTRACT: Reactive oxygen species (ROS) play a crucial role in lipid peroxidation and the initiation of ferroptosis, significantly affecting chemotherapeutic drug resistance. However, the mechanisms by which ROS function and are sensed remain poorly understood. In this study, we identified O-GlcNAc transferase (OGT), a key enzyme in protein O-GlcNAcylation, as a sensor for ROS induced by ferroptosis. The ROS-induced oxidation of OGT at C845 in its catalytic domain activates the enzyme. Once activated, OGT O-GlcNAcylates FOXK2, enhancing its interaction with importin α, which facilitates FOXK2's nuclear translocation and binding to the SLC7A11 promoter region. This, in turn, boosts SLC7A11 transcription, thereby inhibiting ferroptosis. The elevated OGT-FOXK2-SLC7A11 axis contributes to tumorigenesis and resistance to chemoradiotherapy in hepatocellular carcinoma (HCC). Our findings elucidate a ROS-induced oxidation-O-GlcNAcylation cascade that integrates ROS signaling, O-GlcNAcylation, FOXK2-mediated SLC7A11 transcription, and resistance to both ferroptosis and chemoradiotherapy.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Chunyan Hou  

LAB HEAD: Junfeng Ma

PROVIDER: PXD064117 | Pride | 2025-05-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
FOXK2_HCD_EThcD.msf Msf
FOXK2_HCD_EThcD.mzTab Mztab
FOXK2_HCD_EThcD.raw Raw
OGT1_HUMAN.fasta Fasta
OGT_HCD.msf Msf
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