Protein disulfide isomerases regulate androgen receptor stability and promote prostate cancer cell growth and survival

J Jianling Xie (School of Biology and Biological Engineering, South China University of Technology) K Kaikai Shen (School of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine,) W Wenken Liang (School of Biology and Biological Engineering, South China University of Technology) Z Zijian Kuang (School of Biology and Biological Engineering, South China University of Technology) R Raj K. Shrestha (Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health) A Adrienne R. Hanson (Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health) S Scott L. Townley (Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health) M Meiling He (School of Biology and Biological Engineering, South China University of Technology) S Sishu Yu (School of Biology and Biological Engineering, South China University of Technology) P Peiwen Zhou (School of Biology and Biological Engineering, South China University of Technology) L Liangzhen Zhu (Department of Urology, Nanxishan Hospital of Guangxi Zhuang Autonomous Region) Z Zhiwen Gong (School of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine,) X Xiang Ao (School of Biology and Biological Engineering, South China University of Technology) S Sushma R. Rao (Adelaide Medical School, Faculty of Health and Medical Sciences, The University of Adelaide) Q Qing Zhang K Kaijie Chen (School of Biology and Biological Engineering, South China University of Technology) J Jinfen Wei (School of Biology and Biological Engineering, South China University of Technology) S Shashikanth Marri (Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health) M Marten F. Snel (Proteomics, Metabolomics and MS-Imaging Facility, South Australian Health and Medical Research Institute) S Swati Irani (Adelaide Medical School, Faculty of Health and Medical Sciences, The University of Adelaide) L Liye Chen (School of Biology and Biological Engineering, South China University of Technology) L Ling Wang D Daniel P. McDougal (Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide) J John B. Bruning (Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide) M Minglin Ou (Laboratory Center, Guangxi Key Laboratory of Metabolic Reprogramming and Intelligent Medical Engineering for Chronic Diseases, The Second Affiliated Hospital of Guilin Medical University) S Shaobo Wang (Department of Basic Research, Guangzhou National Laboratory, Guangzhou International Bio-Island) C Christopher G. Proud (Lifelong Health Theme, South Australian Health and Medical Research Institute) H Hongli Du (School of Biology and Biological Engineering, South China University of Technology) L Lisa M. Butler L Luke A. Selth (Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health)

Abstract

Cancer cells exhibit accelerated protein production to accommodate their high rates of growth and proliferation. Elevated protein synthesis creates a dependency on endoplasmic reticulum (ER)-resident proteins and chaperones, which are required to maintain proteostasis. In this study, we identified the protein disulfide isomerases (PDIs) PDIA1 and PDIA5, which play a critical role in folding of client proteins in the ER, as important regulators of prostate cancer growth and response to therapy. PDIA1 and PDIA5 are upregulated in prostate cancer and induced by the androgen receptor (AR) signaling axis. Genetic or pharmacological disabling of PDIA1/PDIA5 caused redox stress, mitochondrial dysfunction, growth inhibition, and death of prostate cancer cells in vitro and in vivo. The critical functions of these enzymes in redox homeostasis and cell survival were observed in both AR-driven and AR-independent models of prostate cancer. Loss of PDIA1/PDIA5 activity led to ubiquitination and degradation of the AR, revealing a feedback loop between these chaperones and the AR pathway. Mechanistically, PDIA1/PDIA5 regulated AR stability by mediating disulfide bond formation, an activity that required cysteines 669 and 844 in AR’s ligand-binding domain. Importantly, targeting PDIAs sensitized prostate cancer cells to the AR antagonist, enzalutamide. This study reveals a mechanism governing AR proteostasis in prostate cancer and positions PDIA1/5 as viable therapeutic targets.

Article Details

Volume / Issue Vol. 122, Issue 42
Published October 21, 2025
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (30)

J

Jianling Xie

School of Biology and Biological Engineering, South China University of Technology

K

Kaikai Shen

School of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine,

W

Wenken Liang

School of Biology and Biological Engineering, South China University of Technology

Z

Zijian Kuang

School of Biology and Biological Engineering, South China University of Technology

R

Raj K. Shrestha

Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health

A

Adrienne R. Hanson

Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health

S

Scott L. Townley

Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health

M

Meiling He

School of Biology and Biological Engineering, South China University of Technology

S

Sishu Yu

School of Biology and Biological Engineering, South China University of Technology

P

Peiwen Zhou

School of Biology and Biological Engineering, South China University of Technology

L

Liangzhen Zhu

Department of Urology, Nanxishan Hospital of Guangxi Zhuang Autonomous Region

Z

Zhiwen Gong

School of Traditional Chinese Medicine, Shanghai University of Traditional Chinese Medicine,

X

Xiang Ao

School of Biology and Biological Engineering, South China University of Technology

S

Sushma R. Rao

Adelaide Medical School, Faculty of Health and Medical Sciences, The University of Adelaide

Q

Qing Zhang

K

Kaijie Chen

School of Biology and Biological Engineering, South China University of Technology

J

Jinfen Wei

School of Biology and Biological Engineering, South China University of Technology

S

Shashikanth Marri

Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health

M

Marten F. Snel

Proteomics, Metabolomics and MS-Imaging Facility, South Australian Health and Medical Research Institute

S

Swati Irani

Adelaide Medical School, Faculty of Health and Medical Sciences, The University of Adelaide

L

Liye Chen

School of Biology and Biological Engineering, South China University of Technology

L

Ling Wang

D

Daniel P. McDougal

Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide

J

John B. Bruning

Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide

M

Minglin Ou

Laboratory Center, Guangxi Key Laboratory of Metabolic Reprogramming and Intelligent Medical Engineering for Chronic Diseases, The Second Affiliated Hospital of Guilin Medical University

S

Shaobo Wang

Department of Basic Research, Guangzhou National Laboratory, Guangzhou International Bio-Island

C

Christopher G. Proud

Lifelong Health Theme, South Australian Health and Medical Research Institute

H

Hongli Du

School of Biology and Biological Engineering, South China University of Technology

L

Lisa M. Butler

L

Luke A. Selth

Flinders Health and Medical Research Institute, Flinders University, College of Medicine and Public Health