Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆

Loss of β-catenin homeostasis is tightly associated with human malignancies, modulation of β-catenin stabilization could be an attractive strategy for cancer therapy. In the present study, we demonstrated that an ancient drug curcumin was associated with selective accumulation of phosphorylated β-ca...

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Main Authors: Mengzhen Shen, Lizhe Chen, Jie Jiang, Ziye Wang, Qing Gong, Xue Zhang, Xisong Ke, Yi Qu
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Pharmacological Research
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Online Access:http://www.sciencedirect.com/science/article/pii/S1043661825001707
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author Mengzhen Shen
Lizhe Chen
Jie Jiang
Ziye Wang
Qing Gong
Xue Zhang
Xisong Ke
Yi Qu
author_facet Mengzhen Shen
Lizhe Chen
Jie Jiang
Ziye Wang
Qing Gong
Xue Zhang
Xisong Ke
Yi Qu
author_sort Mengzhen Shen
collection DOAJ
description Loss of β-catenin homeostasis is tightly associated with human malignancies, modulation of β-catenin stabilization could be an attractive strategy for cancer therapy. In the present study, we demonstrated that an ancient drug curcumin was associated with selective accumulation of phosphorylated β-catenin (PBC) tagged with both ubiquitin (Ub) and Ub-like (Ubl) protein NEDD8. We further identified USP14, a deubiquitinating enzyme (DUB) in 19S proteasome, as a functional target of curcumin in modulating β-catenin. Curcumin enhances USP14-mediated PBC trapping and modulates proteasome associations, loss of USP14 significantly attenuated curcumin-increased PBC. Additionally, we found that USP14 deficiency suppressed mitotic entry and cell proliferation, targeting USP14 and PBC was essential for curcumin inhibition of cancer. Taken together, our study not only revealed the association of USP14 with PBC degradation within the proteasome, but also provided a unique small molecule curcumin targeting USP14 to modulate β-catenin for cancer therapy.
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publishDate 2025-06-01
publisher Elsevier
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series Pharmacological Research
spelling doaj-art-7bed6a82de3f4d35b0df13e6e8a568a72025-08-20T02:02:01ZengElsevierPharmacological Research1096-11862025-06-0121610774510.1016/j.phrs.2025.107745Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆Mengzhen Shen0Lizhe Chen1Jie Jiang2Ziye Wang3Qing Gong4Xue Zhang5Xisong Ke6Yi Qu7Center for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCenter for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCenter for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCenter for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCenter for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCorrespondence to: No.1200, Cailun Road, Shanghai 201203, PR China; Center for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCorrespondence to: No.1200, Cailun Road, Shanghai 201203, PR China; Center for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaCorrespondence to: No.1200, Cailun Road, Shanghai 201203, PR China; Center for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, PR ChinaLoss of β-catenin homeostasis is tightly associated with human malignancies, modulation of β-catenin stabilization could be an attractive strategy for cancer therapy. In the present study, we demonstrated that an ancient drug curcumin was associated with selective accumulation of phosphorylated β-catenin (PBC) tagged with both ubiquitin (Ub) and Ub-like (Ubl) protein NEDD8. We further identified USP14, a deubiquitinating enzyme (DUB) in 19S proteasome, as a functional target of curcumin in modulating β-catenin. Curcumin enhances USP14-mediated PBC trapping and modulates proteasome associations, loss of USP14 significantly attenuated curcumin-increased PBC. Additionally, we found that USP14 deficiency suppressed mitotic entry and cell proliferation, targeting USP14 and PBC was essential for curcumin inhibition of cancer. Taken together, our study not only revealed the association of USP14 with PBC degradation within the proteasome, but also provided a unique small molecule curcumin targeting USP14 to modulate β-catenin for cancer therapy.http://www.sciencedirect.com/science/article/pii/S1043661825001707Curcuminβ-catenin stabilizationUSP14proteasomecolorectal cancer
spellingShingle Mengzhen Shen
Lizhe Chen
Jie Jiang
Ziye Wang
Qing Gong
Xue Zhang
Xisong Ke
Yi Qu
Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
Pharmacological Research
Curcumin
β-catenin stabilization
USP14
proteasome
colorectal cancer
title Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
title_full Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
title_fullStr Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
title_full_unstemmed Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
title_short Curcumin modulates β-catenin stabilization via targeting proteasomal deubiquitinating enzyme USP14☆
title_sort curcumin modulates β catenin stabilization via targeting proteasomal deubiquitinating enzyme usp14☆
topic Curcumin
β-catenin stabilization
USP14
proteasome
colorectal cancer
url http://www.sciencedirect.com/science/article/pii/S1043661825001707
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