Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke

Abstract As a common and severe cerebrovascular disease, ischemic stroke casts a significant shadow over global health. Unfortunately, the mechanisms regulating neuronal death in the affected areas remain largely unclear. Here, we found that deletion of the deubiquitinating enzyme Otubain-2 (OTUB2)...

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Main Authors: Fuqi Mei, Deyu Deng, Zijun Cao, Liyan Lou, Kangmin Chen, Minjie Hu, Zhenhu Zhu, Jiangyun Shen, Jianzhao Zhang, Jie Liang, Jingyong Huang, Min Bao, Ari Waisman, Xu Wang
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Language:English
Published: Springer Nature 2025-02-01
Series:EMBO Molecular Medicine
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Online Access:https://doi.org/10.1038/s44321-025-00206-6
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author Fuqi Mei
Deyu Deng
Zijun Cao
Liyan Lou
Kangmin Chen
Minjie Hu
Zhenhu Zhu
Jiangyun Shen
Jianzhao Zhang
Jie Liang
Jingyong Huang
Min Bao
Ari Waisman
Xu Wang
author_facet Fuqi Mei
Deyu Deng
Zijun Cao
Liyan Lou
Kangmin Chen
Minjie Hu
Zhenhu Zhu
Jiangyun Shen
Jianzhao Zhang
Jie Liang
Jingyong Huang
Min Bao
Ari Waisman
Xu Wang
author_sort Fuqi Mei
collection DOAJ
description Abstract As a common and severe cerebrovascular disease, ischemic stroke casts a significant shadow over global health. Unfortunately, the mechanisms regulating neuronal death in the affected areas remain largely unclear. Here, we found that deletion of the deubiquitinating enzyme Otubain-2 (OTUB2) significantly alleviated ischemia-induced cerebral infarction and neurological deficits, accompanied by a reduction in neuronal loss, glial activation, and neuroinflammation. OTUB2 was predominantly expressed in neurons and its deletion decreased receptor-interacting protein kinase 3 (RIPK3)-mediated neuronal necroptosis. Moreover, OTUB2 increased RIPK3 protein abundance by inhibiting the proteasomal degradation of RIPK3. Mechanistically, OTUB2 removed K48-linked polyubiquitin chains from RIPK3 through its active site C51. Importantly, pharmacological inhibition of OTUB2 alleviated ischemic brain injury in mice and reduced oxygen-glucose deprivation-induced neuronal death in human brain organoids. These results demonstrate that OTUB2 critically regulates ischemic stroke injury by potentiating neuronal necroptosis, suggesting that OTUB2 inhibition may become a potential therapeutic approach for treating ischemic stroke.
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spelling doaj-art-4231de83bdfd4aaa9a33ce95612fda7a2025-08-20T02:28:04ZengSpringer NatureEMBO Molecular Medicine1757-46842025-02-0117467969510.1038/s44321-025-00206-6Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic strokeFuqi Mei0Deyu Deng1Zijun Cao2Liyan Lou3Kangmin Chen4Minjie Hu5Zhenhu Zhu6Jiangyun Shen7Jianzhao Zhang8Jie Liang9Jingyong Huang10Min Bao11Ari Waisman12Xu Wang13School of Pharmaceutical Sciences, Wenzhou Medical UniversitySchool of Pharmaceutical Sciences, Wenzhou Medical UniversitySchool of Pharmaceutical Sciences, Wenzhou Medical UniversitySchool of Pharmaceutical Sciences, Wenzhou Medical UniversitySchool of Pharmaceutical Sciences, Wenzhou Medical UniversityOujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision, and Brain Health)Oujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision, and Brain Health)Oujiang Laboratory (Zhejiang Lab for Regenerative Medicine, Vision, and Brain Health)School of Pharmaceutical Sciences, Wenzhou Medical UniversityDepartment of Rehabilitation, Central Hospital of Jinhua CityDepartment of Vascular Surgery, The First Affiliated Hospital of Wenzhou Medical UniversityOujiang Laboratory, The First Affiliated Hospital of Wenzhou Medical UniversityInstitute for Molecular Medicine, Johannes Gutenberg University MainzSchool of Pharmaceutical Sciences, Wenzhou Medical UniversityAbstract As a common and severe cerebrovascular disease, ischemic stroke casts a significant shadow over global health. Unfortunately, the mechanisms regulating neuronal death in the affected areas remain largely unclear. Here, we found that deletion of the deubiquitinating enzyme Otubain-2 (OTUB2) significantly alleviated ischemia-induced cerebral infarction and neurological deficits, accompanied by a reduction in neuronal loss, glial activation, and neuroinflammation. OTUB2 was predominantly expressed in neurons and its deletion decreased receptor-interacting protein kinase 3 (RIPK3)-mediated neuronal necroptosis. Moreover, OTUB2 increased RIPK3 protein abundance by inhibiting the proteasomal degradation of RIPK3. Mechanistically, OTUB2 removed K48-linked polyubiquitin chains from RIPK3 through its active site C51. Importantly, pharmacological inhibition of OTUB2 alleviated ischemic brain injury in mice and reduced oxygen-glucose deprivation-induced neuronal death in human brain organoids. These results demonstrate that OTUB2 critically regulates ischemic stroke injury by potentiating neuronal necroptosis, suggesting that OTUB2 inhibition may become a potential therapeutic approach for treating ischemic stroke.https://doi.org/10.1038/s44321-025-00206-6Ischemic StrokeNecroptosisUbiquitinationOTUB2RIPK3
spellingShingle Fuqi Mei
Deyu Deng
Zijun Cao
Liyan Lou
Kangmin Chen
Minjie Hu
Zhenhu Zhu
Jiangyun Shen
Jianzhao Zhang
Jie Liang
Jingyong Huang
Min Bao
Ari Waisman
Xu Wang
Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
EMBO Molecular Medicine
Ischemic Stroke
Necroptosis
Ubiquitination
OTUB2
RIPK3
title Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
title_full Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
title_fullStr Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
title_full_unstemmed Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
title_short Deubiquitination of RIPK3 by OTUB2 potentiates neuronal necroptosis after ischemic stroke
title_sort deubiquitination of ripk3 by otub2 potentiates neuronal necroptosis after ischemic stroke
topic Ischemic Stroke
Necroptosis
Ubiquitination
OTUB2
RIPK3
url https://doi.org/10.1038/s44321-025-00206-6
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