CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer

Abstract We previously identified CLDN6 as a pivotal tumor suppressor in breast cancer and unexpectedly discovered that overexpression of CLDN6 resulted in characteristic ultrastructural alterations of ferroptosis. However, the exact mechanism by which CLDN6 triggers ferroptosis is still elusive in...

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Main Authors: Da Qi, Yan Lu, Huinan Qu, Yuan Dong, Qiu Jin, Minghao Sun, Chengshi Quan
Format: Article
Language:English
Published: Nature Publishing Group 2025-02-01
Series:Cell Death and Disease
Online Access:https://doi.org/10.1038/s41419-025-07448-9
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author Da Qi
Yan Lu
Huinan Qu
Yuan Dong
Qiu Jin
Minghao Sun
Chengshi Quan
author_facet Da Qi
Yan Lu
Huinan Qu
Yuan Dong
Qiu Jin
Minghao Sun
Chengshi Quan
author_sort Da Qi
collection DOAJ
description Abstract We previously identified CLDN6 as a pivotal tumor suppressor in breast cancer and unexpectedly discovered that overexpression of CLDN6 resulted in characteristic ultrastructural alterations of ferroptosis. However, the exact mechanism by which CLDN6 triggers ferroptosis is still elusive in breast cancer. Our study showed that CLDN6 was associated with ferroptosis in breast cancer patients. The integration of CLDN6 and ferroptosis demonstrated remarkable predictive prognostic performance. We observed that CLDN6 triggers NRF2-mediated ferroptosis in vitro and in vivo. Mechanistically, CLDN6 enhanced nuclear export of NRF2 by regulating the PBK-dependent AKT/GSK3β/FYN axis. Further CLDN6 recruited PBK to the cell membrane through the endosomal pathway and bound with the DLG1/PBK complex, thereby promoted the degradation of PBK by the UPS. This study elucidates the previously unrecognized mechanism of CLDN6 triggering NRF2-mediated ferroptosis through recruiting DLG1/PBK complex. This study provides a reliable biomarker for predicting prognosis and is anticipated to guide the selection of therapies targeting ferroptosis in breast cancer.
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institution Kabale University
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language English
publishDate 2025-02-01
publisher Nature Publishing Group
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series Cell Death and Disease
spelling doaj-art-063b4f176e7e4f1e952d1ab4cf19b58d2025-08-24T11:54:21ZengNature Publishing GroupCell Death and Disease2041-48892025-02-0116111110.1038/s41419-025-07448-9CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancerDa Qi0Yan Lu1Huinan Qu2Yuan Dong3Qiu Jin4Minghao Sun5Chengshi Quan6The Key Laboratory of Pathobiology, Ministry of Education, College of Basic Medical Sciences, Jilin UniversityDepartment of Anatomy, College of Basic Medical Sciences, Jilin UniversityDepartment of Histology and Embryology, College of Basic Medical Sciences, Jilin UniversityThe Key Laboratory of Pathobiology, Ministry of Education, College of Basic Medical Sciences, Jilin UniversityThe Key Laboratory of Pathobiology, Ministry of Education, College of Basic Medical Sciences, Jilin UniversityThe Key Laboratory of Pathobiology, Ministry of Education, College of Basic Medical Sciences, Jilin UniversityThe Key Laboratory of Pathobiology, Ministry of Education, College of Basic Medical Sciences, Jilin UniversityAbstract We previously identified CLDN6 as a pivotal tumor suppressor in breast cancer and unexpectedly discovered that overexpression of CLDN6 resulted in characteristic ultrastructural alterations of ferroptosis. However, the exact mechanism by which CLDN6 triggers ferroptosis is still elusive in breast cancer. Our study showed that CLDN6 was associated with ferroptosis in breast cancer patients. The integration of CLDN6 and ferroptosis demonstrated remarkable predictive prognostic performance. We observed that CLDN6 triggers NRF2-mediated ferroptosis in vitro and in vivo. Mechanistically, CLDN6 enhanced nuclear export of NRF2 by regulating the PBK-dependent AKT/GSK3β/FYN axis. Further CLDN6 recruited PBK to the cell membrane through the endosomal pathway and bound with the DLG1/PBK complex, thereby promoted the degradation of PBK by the UPS. This study elucidates the previously unrecognized mechanism of CLDN6 triggering NRF2-mediated ferroptosis through recruiting DLG1/PBK complex. This study provides a reliable biomarker for predicting prognosis and is anticipated to guide the selection of therapies targeting ferroptosis in breast cancer.https://doi.org/10.1038/s41419-025-07448-9
spellingShingle Da Qi
Yan Lu
Huinan Qu
Yuan Dong
Qiu Jin
Minghao Sun
Chengshi Quan
CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
Cell Death and Disease
title CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
title_full CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
title_fullStr CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
title_full_unstemmed CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
title_short CLDN6 triggers NRF2-mediated ferroptosis through recruiting DLG1/PBK complex in breast cancer
title_sort cldn6 triggers nrf2 mediated ferroptosis through recruiting dlg1 pbk complex in breast cancer
url https://doi.org/10.1038/s41419-025-07448-9
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