The Interaction of OTUB1 and TRAF3 Mediates NLRP3 Inflammasome Activity to Regulate TGF-β1-induced BEAS-2B Cell Injury

Shang, Liqun; Du, Yong‐Zhong; Zhao, Yue; Zhang, Yongqing; Liu, Cuicui

doi:10.1007/s12010-023-04434-9

Cited by 2 publications

(1 citation statement)

References 56 publications

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“…Consequently, this inhibited the bronchial epithelial cell inflammatory response, proliferation, apoptosis, migration, and epithelial–mesenchymal transition. However, overexpressing TRAF3 was found to be damaging to human bronchial epithelial cells [ 95 ]. In conclusion, the ubiquitination or deubiquitination of NLRP3 inflammasomes plays a critical role in inhibiting abnormal cell proliferation and plays a protective role against inflammation ( Figure 2 ).…”

Section: Potential Mechanisms Of Nlrp3 Inflammasome Ubiquitination/ D...mentioning

confidence: 99%

The roles of ubiquitination and deubiquitination of NLRP3 inflammasome in inflammation-related diseases: A review

Tang,

Geng,

Wang

et al. 2024

Biomol Biomed

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The inflammatory response is a natural immune response that prevents microbial invasion and repairs damaged tissues. However, excessive inflammatory responses can lead to various inflammation-related diseases, posing a significant threat to human health. The NOD-like receptor pyrin domain-containing protein 3 (NLRP3) inflammasome is a vital mediator in the activation of the inflammatory cascade. Targeting the hyperactivation of the NLRP3 inflammasome may offer potential strategies for the prevention or treatment of inflammation-related diseases. It has been established that the ubiquitination and deubiquitination modifications of the NLRP3 inflammasome can provide protective effects in inflammation-related diseases. These modifications modulate several pathological processes, including excessive inflammatory responses, pyroptosis, abnormal autophagy, proliferation disorders, and oxidative stress damage. Therefore, this review discusses the regulation of NLRP3 inflammasome activation by ubiquitination and deubiquitination modifications, explores the role of these modifications in inflammation-related diseases, and examines the potential underlying mechanisms.

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Section: Potential Mechanisms Of Nlrp3 Inflammasome Ubiquitination/ D...mentioning

confidence: 99%

The roles of ubiquitination and deubiquitination of NLRP3 inflammasome in inflammation-related diseases: A review

Tang,

Geng,

Wang

et al. 2024

Biomol Biomed

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Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases

Bolhuis,

Emanuele,

Brown

2024

Biochemical Society Transactions

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Protein ubiquitination is a post-translational modification that entails the covalent attachment of the small protein ubiquitin (Ub), which acts as a signal to direct protein stability, localization, or interactions. The Ub code is written by a family of enzymes called E3 Ub ligases (∼600 members in humans), which can catalyze the transfer of either a single ubiquitin or the formation of a diverse array of polyubiquitin chains. This code can be edited or erased by a different set of enzymes termed deubiquitinases (DUBs; ∼100 members in humans). While enzymes from these distinct families have seemingly opposing activities, certain E3–DUB pairings can also synergize to regulate vital cellular processes like gene expression, autophagy, innate immunity, and cell proliferation. In this review, we highlight recent studies describing Ub ligase-DUB interactions and focus on their relationships.

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The Interaction of OTUB1 and TRAF3 Mediates NLRP3 Inflammasome Activity to Regulate TGF-β1-induced BEAS-2B Cell Injury

Cited by 2 publications

References 56 publications

The roles of ubiquitination and deubiquitination of NLRP3 inflammasome in inflammation-related diseases: A review

The roles of ubiquitination and deubiquitination of NLRP3 inflammasome in inflammation-related diseases: A review

Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases

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