Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling

Abstract Background Phosphoglycerate kinase 1 (PGK1) serves as a critical metabolic enzyme in the process of glycolysis and has many nonmetabolic functions in tumour progression. One of the most prevalent malignant tumours is still esophageal squamous cell carcinoma (ESCC), with high recurrence rate...

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Main Authors: Jia‐cheng Xu, Lin‐feng Wu, Tian‐yin Chen, Yan‐bo Liu, Yi‐fei Zhang, Ping‐hong Zhou, Yi‐qun Zhang
Format: Article
Language:English
Published: Wiley 2025-06-01
Series:Clinical and Translational Medicine
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Online Access:https://doi.org/10.1002/ctm2.70376
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author Jia‐cheng Xu
Lin‐feng Wu
Tian‐yin Chen
Yan‐bo Liu
Yi‐fei Zhang
Ping‐hong Zhou
Yi‐qun Zhang
author_facet Jia‐cheng Xu
Lin‐feng Wu
Tian‐yin Chen
Yan‐bo Liu
Yi‐fei Zhang
Ping‐hong Zhou
Yi‐qun Zhang
author_sort Jia‐cheng Xu
collection DOAJ
description Abstract Background Phosphoglycerate kinase 1 (PGK1) serves as a critical metabolic enzyme in the process of glycolysis and has many nonmetabolic functions in tumour progression. One of the most prevalent malignant tumours is still esophageal squamous cell carcinoma (ESCC), with high recurrence rates, high probabilities of metastasis, and poor prognoses. However, the molecular mechanisms and physiological contribution of PGK1 to ESCC carcinogenesis remain largely elusive. Methods Esophageal cancer bioinformatics analysis and tissue microarray analysis were employed to elucidate the aberrant expression of PGK1 during ESCC progression. The carcinogenic effect of PGK1 was examined using cell proliferation, migration and sphere formation assays. Mass spectrometry analysis, immunoprecipitation, ChIP and luciferase assays, hypoxia assays and in vitro and in vivo experiments were used to clarify the mechanism of the PGK1‒MYH9 interaction in the β‐catenin/c‐Myc signalling pathway. Results We clarified that in patients with ESCC, elevated PGK1 levels were linked to poor survival, tumour size, lymph node metastatic status, and TNM stage. In vivo and in vitro experimental analyses revealed that PGK1 promoted ESCC cell tumour stemness and EMT both in vivo and in vitro. Mechanistically, we discovered that PGK1 interacts with myosin‐9 (MYH9), leading to MYH9‐mediated ubiquitination‐mediated degradation of GSK‐3β, thereby triggering the β‐catenin signalling pathway and transcriptionally increasing c‐Myc expression. In addition, we found that hypoxic conditions upregulated PGK1, with HIF‐1α transactivating PGK1 expression, further promoting the PGK1‐MYH9 interaction and PGK1/MYH9/β‐catenin/c‐Myc axis activation. Conclusions PGK1 promotes ESCC tumourigenicity and migratory capacity by facilitating β‐catenin‐dependent c‐Myc transcription. Under hypoxic conditions, the PGK1‒MYH9 interaction is strengthened, and HIF‐1α‐mediated transcription increases PGK1 expression, thereby activating the β‐catenin/c‐Myc signalling pathway. Taken together, PGK1 holds promise as a potential biomarker for predicting postoperative prognosis and recurrence in patients with ESCC.
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spelling doaj-art-bffadc47d4af41a8b71df1bd4450099c2025-08-20T03:23:56ZengWileyClinical and Translational Medicine2001-13262025-06-01156n/an/a10.1002/ctm2.70376Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signallingJia‐cheng Xu0Lin‐feng Wu1Tian‐yin Chen2Yan‐bo Liu3Yi‐fei Zhang4Ping‐hong Zhou5Yi‐qun Zhang6Department of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaDepartment of Endoscopy Center and Endoscopy Research Institute Zhongshan Hospital Fudan University Shanghai ChinaAbstract Background Phosphoglycerate kinase 1 (PGK1) serves as a critical metabolic enzyme in the process of glycolysis and has many nonmetabolic functions in tumour progression. One of the most prevalent malignant tumours is still esophageal squamous cell carcinoma (ESCC), with high recurrence rates, high probabilities of metastasis, and poor prognoses. However, the molecular mechanisms and physiological contribution of PGK1 to ESCC carcinogenesis remain largely elusive. Methods Esophageal cancer bioinformatics analysis and tissue microarray analysis were employed to elucidate the aberrant expression of PGK1 during ESCC progression. The carcinogenic effect of PGK1 was examined using cell proliferation, migration and sphere formation assays. Mass spectrometry analysis, immunoprecipitation, ChIP and luciferase assays, hypoxia assays and in vitro and in vivo experiments were used to clarify the mechanism of the PGK1‒MYH9 interaction in the β‐catenin/c‐Myc signalling pathway. Results We clarified that in patients with ESCC, elevated PGK1 levels were linked to poor survival, tumour size, lymph node metastatic status, and TNM stage. In vivo and in vitro experimental analyses revealed that PGK1 promoted ESCC cell tumour stemness and EMT both in vivo and in vitro. Mechanistically, we discovered that PGK1 interacts with myosin‐9 (MYH9), leading to MYH9‐mediated ubiquitination‐mediated degradation of GSK‐3β, thereby triggering the β‐catenin signalling pathway and transcriptionally increasing c‐Myc expression. In addition, we found that hypoxic conditions upregulated PGK1, with HIF‐1α transactivating PGK1 expression, further promoting the PGK1‐MYH9 interaction and PGK1/MYH9/β‐catenin/c‐Myc axis activation. Conclusions PGK1 promotes ESCC tumourigenicity and migratory capacity by facilitating β‐catenin‐dependent c‐Myc transcription. Under hypoxic conditions, the PGK1‒MYH9 interaction is strengthened, and HIF‐1α‐mediated transcription increases PGK1 expression, thereby activating the β‐catenin/c‐Myc signalling pathway. Taken together, PGK1 holds promise as a potential biomarker for predicting postoperative prognosis and recurrence in patients with ESCC.https://doi.org/10.1002/ctm2.70376β‐catenin signalling pathwayesophageal squamous cell carcinomahypoxiaMYH9PGK1
spellingShingle Jia‐cheng Xu
Lin‐feng Wu
Tian‐yin Chen
Yan‐bo Liu
Yi‐fei Zhang
Ping‐hong Zhou
Yi‐qun Zhang
Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
Clinical and Translational Medicine
β‐catenin signalling pathway
esophageal squamous cell carcinoma
hypoxia
MYH9
PGK1
title Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
title_full Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
title_fullStr Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
title_full_unstemmed Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
title_short Hypoxia‐induced PGK1 expression promotes esophageal squamous cell carcinoma progression via stimulating MYH9‐mediated GSK3β/β‐catenin signalling
title_sort hypoxia induced pgk1 expression promotes esophageal squamous cell carcinoma progression via stimulating myh9 mediated gsk3β β catenin signalling
topic β‐catenin signalling pathway
esophageal squamous cell carcinoma
hypoxia
MYH9
PGK1
url https://doi.org/10.1002/ctm2.70376
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