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PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11 [scRNA-seq]

ABSTRACT: Comparative gene expression profiling analysis of scRNA-seq data for PGK1 KO and PGK1 WT HCC cells

ORGANISM(S): Mus musculus

PROVIDER: GSE317778 | GEO | 2026/07/12

REPOSITORIES: GEO

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PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11

Project description:Ferroptosis is restrained by layered antioxidant defenses, yet whether glycolytic enzymes directly constitute ferroptosis-defense machinery remains unclear. Here we identify phosphoglycerate kinase 1 (PGK1) as a non-canonical suppressor of ferroptosis that functions independently of its glycolytic kinase activity. Across pan-cancer bulk and single-cell transcriptomes, glycolysis inversely associates with ferroptosis programs, with PGK1 emerging as a prognostic hub. PGK1 loss in multiple tumor models elicits hallmark ferroptotic features, elevates lipid peroxidation and labile iron, and suppresses xenograft growth, all of which are reversed by liproxstatin-1. Mechanistically, PGK1 physically binds the C-terminal tail of SLC7A11 (aa 471-501) and shields it from ubiquitin-proteasome degradation, thereby sustaining cystine-driven glutathione synthesis and redox homeostasis. This scaffolding role is preserved in a kinase-dead PGK1 mutant, establishing a strict separation between metabolic and ferroptosis-regulatory functions. Restoring SLC7A11 rescues PGK1-deficient tumor growth, whereas a rationally designed competing peptide SLC7A11471-501 (FP-01) disrupts the PGK1-SLC7A11 interface, depletes SLC7A11/GSH, triggers ferroptosis, and suppresses tumor progression in vivo. Collectively, the PGK1-SLC7A11 interaction represents a druggable ferroptosis vulnerability that enables selective ferroptosis induction while sparing essential glycolysis.

2026-07-12 | GSE317428 | GEO

PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11 [RNA-Seq]

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PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11

Project description:PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11

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PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11

Project description:PGK1 acts as a non-catalytic gatekeeper of ferroptosis by stabilizing SLC7A11

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Novel PGK1 determines AR stability dependent on Spk2 and reprograms granular cell glucose metabolism to facilitate ovulation dysfunction

Project description:Ovulation disorder is the main characteristic of polycystic ovary syndrome (PCOS), but the concrete molecular mechanism is unclear. Phosphoglycerate kinase 1 (PGK1) plays an important role in the process of glycolytic cycles. Androgen and androgen receptor (AR) are considered as one of the critical factors in the prevalence of hyperandrogenemia and follicular development, and whether PGK1 participates in the metabolic reaction via AR in PCOS remains vague. PGK1 and AR proteins were highly expressed in PCOS luteinized granulosa cells and the PCOS-like mice ovary tissues. PGK1 increased lactate levels and deteriorated PCOS-like mouse metabolic disorder, and importantly, the phenotype of PCOS-like mice was rescued by PTX (paclitaxel) and the PGK1 and AR protein levels also decreased in the ovary. We demonstrated that PGK1 promoted AR translocation into the nuclear, and PGK1 was dependent on the E3 ligase Skp2 to repress the AR ubiquitination to improve the AR stability. In addition, we found that follicular development critical genes MAP2K6, KLF15, LRIG3 and MYOF were regulated by the PGK1-AR axis in the RNA-seq data, and axis also mediated cell proliferation and apoptosis. This study highlights the glycolysis key gene PGK1 to regulate metabolism in granular cell result in etiology of the PCOS. The PGK1-AR axis might provide a new therapy target of PCOS

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Site mapping of PGK1 O-GlcNAcylation

Project description:To identify the site(s) of O-GlcNAcylation on PGK1, we transiently co-expressed Flag-tagged PGK1 and OGT in HEK293T cells. After immunoprecipitation using anti-Flag M2 beads and in-gel trypsin digestion, resulted peptides were subjected to mass spectrometry analysis

2019-11-06 | PXD015659 | Pride