HECTD3 inhibits NLRP3 inflammasome assembly and activation by blocking NLRP3-NEK7 interaction
The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been r...
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Published in | Cell death & disease Vol. 15; no. 1; p. 86 |
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Main Authors | , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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England
Springer Nature B.V
24.01.2024
Nature Publishing Group UK Nature Publishing Group |
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Abstract | The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been reported to participate in autoimmune and infectious diseases. However, the relationship between HECTD3 and the NLRP3 inflammasome has not been well studied. Herein, we show that HECTD3 blocks the interaction between NEK7 and NLRP3 to inhibit NLRP3 inflammasome assembly and activation. In BMDMs, Hectd3 deficiency promotes the assembly and activation of NLRP3 inflammasome and the secretion of IL-1β, while the overexpression of HECTD3 inhibits these processes. Unexpectedly, HECTD3 functions in an E3 activity independent manner. Mechanically, the DOC domain of HECTD3 interacts with NACHT/LRR domain of NLRP3, which blocks NLRP3-NEK7 interaction and NLRP3 oligomerization. Furthermore, HECTD3 inhibits monosodium urate crystals (MSU)-induced gouty arthritis, a NLRP3-related disease. Thus, we reveal a novel regulatory mechanism of NLRP3 by HECTD3 and suggest HECTD3 could be a potential therapeutic target for NLRP3-dependent pathologies. |
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AbstractList | The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been reported to participate in autoimmune and infectious diseases. However, the relationship between HECTD3 and the NLRP3 inflammasome has not been well studied. Herein, we show that HECTD3 blocks the interaction between NEK7 and NLRP3 to inhibit NLRP3 inflammasome assembly and activation. In BMDMs, Hectd3 deficiency promotes the assembly and activation of NLRP3 inflammasome and the secretion of IL-1β, while the overexpression of HECTD3 inhibits these processes. Unexpectedly, HECTD3 functions in an E3 activity independent manner. Mechanically, the DOC domain of HECTD3 interacts with NACHT/LRR domain of NLRP3, which blocks NLRP3-NEK7 interaction and NLRP3 oligomerization. Furthermore, HECTD3 inhibits monosodium urate crystals (MSU)-induced gouty arthritis, a NLRP3-related disease. Thus, we reveal a novel regulatory mechanism of NLRP3 by HECTD3 and suggest HECTD3 could be a potential therapeutic target for NLRP3-dependent pathologies. The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been reported to participate in autoimmune and infectious diseases. However, the relationship between HECTD3 and the NLRP3 inflammasome has not been well studied. Herein, we show that HECTD3 blocks the interaction between NEK7 and NLRP3 to inhibit NLRP3 inflammasome assembly and activation. In BMDMs, Hectd3 deficiency promotes the assembly and activation of NLRP3 inflammasome and the secretion of IL-1β, while the overexpression of HECTD3 inhibits these processes. Unexpectedly, HECTD3 functions in an E3 activity independent manner. Mechanically, the DOC domain of HECTD3 interacts with NACHT/LRR domain of NLRP3, which blocks NLRP3-NEK7 interaction and NLRP3 oligomerization. Furthermore, HECTD3 inhibits monosodium urate crystals (MSU)-induced gouty arthritis, a NLRP3-related disease. Thus, we reveal a novel regulatory mechanism of NLRP3 by HECTD3 and suggest HECTD3 could be a potential therapeutic target for NLRP3-dependent pathologies. Abstract The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been reported to participate in autoimmune and infectious diseases. However, the relationship between HECTD3 and the NLRP3 inflammasome has not been well studied. Herein, we show that HECTD3 blocks the interaction between NEK7 and NLRP3 to inhibit NLRP3 inflammasome assembly and activation. In BMDMs, Hectd3 deficiency promotes the assembly and activation of NLRP3 inflammasome and the secretion of IL-1β, while the overexpression of HECTD3 inhibits these processes. Unexpectedly, HECTD3 functions in an E3 activity independent manner. Mechanically, the DOC domain of HECTD3 interacts with NACHT/LRR domain of NLRP3, which blocks NLRP3-NEK7 interaction and NLRP3 oligomerization. Furthermore, HECTD3 inhibits monosodium urate crystals (MSU)-induced gouty arthritis, a NLRP3-related disease. Thus, we reveal a novel regulatory mechanism of NLRP3 by HECTD3 and suggest HECTD3 could be a potential therapeutic target for NLRP3-dependent pathologies. Abstract The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely understood. Dysregulation of NLRP3 can cause diverse inflammatory diseases. HECTD3 is a E3 ubiquitin ligase of the HECT family that has been reported to participate in autoimmune and infectious diseases. However, the relationship between HECTD3 and the NLRP3 inflammasome has not been well studied. Herein, we show that HECTD3 blocks the interaction between NEK7 and NLRP3 to inhibit NLRP3 inflammasome assembly and activation. In BMDMs, Hectd3 deficiency promotes the assembly and activation of NLRP3 inflammasome and the secretion of IL-1β, while the overexpression of HECTD3 inhibits these processes. Unexpectedly, HECTD3 functions in an E3 activity independent manner. Mechanically, the DOC domain of HECTD3 interacts with NACHT/LRR domain of NLRP3, which blocks NLRP3-NEK7 interaction and NLRP3 oligomerization. Furthermore, HECTD3 inhibits monosodium urate crystals (MSU)-induced gouty arthritis, a NLRP3-related disease. Thus, we reveal a novel regulatory mechanism of NLRP3 by HECTD3 and suggest HECTD3 could be a potential therapeutic target for NLRP3-dependent pathologies. |
ArticleNumber | 86 |
Author | Zeng, Li Cheng, Zhuo Hou, Lei Li, Wei Fan, Qijin Yang, Chuanyu Liang, Bin Li, Fubing Chen, Ceshi Huang, Maobo Li, Chengbin Jin, Li Zhang, Linqiang |
Author_xml | – sequence: 1 givenname: Zhuo surname: Cheng fullname: Cheng, Zhuo organization: Kunming College of Life Sciences, University of Chinese Academy Sciences, Kunming, 650204, China – sequence: 2 givenname: Maobo surname: Huang fullname: Huang, Maobo organization: The First People's Hospital of Kunming City & Calmette Affiliated Hospital of Kunming Medical University, Kunming, 650032, Yunnan, China – sequence: 3 givenname: Wei surname: Li fullname: Li, Wei organization: Kunming College of Life Sciences, University of Chinese Academy Sciences, Kunming, 650204, China – sequence: 4 givenname: Lei surname: Hou fullname: Hou, Lei organization: Department of Breast Disease, Henan Breast Cancer Center, Affiliated Cancer Hospital of Zhengzhou University & Henan Cancer Hospital, Zhengzhou, 450008, China – sequence: 5 givenname: Li surname: Jin fullname: Jin, Li organization: The First Affiliated Hospital, Kunming Medical University, Kunming, 650032, China – sequence: 6 givenname: Qijin surname: Fan fullname: Fan, Qijin organization: College of Life Sciences, Yunnan University, Kunming, 650500, China – sequence: 7 givenname: Linqiang surname: Zhang fullname: Zhang, Linqiang organization: College of Life Sciences, Yunnan University, Kunming, 650500, China – sequence: 8 givenname: Chengbin surname: Li fullname: Li, Chengbin organization: College of Life Sciences, Yunnan University, Kunming, 650500, China – sequence: 9 givenname: Li surname: Zeng fullname: Zeng, Li organization: Kunming College of Life Sciences, University of Chinese Academy Sciences, Kunming, 650204, China – sequence: 10 givenname: Chuanyu surname: Yang fullname: Yang, Chuanyu organization: Kunming College of Life Sciences, University of Chinese Academy Sciences, Kunming, 650204, China – sequence: 11 givenname: Bin surname: Liang fullname: Liang, Bin organization: College of Life Sciences, Yunnan University, Kunming, 650500, China – sequence: 12 givenname: Fubing surname: Li fullname: Li, Fubing email: mtlfb0408@163.com organization: Academy of Biomedical Engineering, Kunming Medical University, Kunming, 650500, China. mtlfb0408@163.com – sequence: 13 givenname: Ceshi orcidid: 0000-0001-6398-3516 surname: Chen fullname: Chen, Ceshi email: chenc@kmmu.edu.cn, chenc@kmmu.edu.cn, chenc@kmmu.edu.cn organization: The Third Affiliated Hospital, Kunming Medical University, Kunming, 650118, China. chenc@kmmu.edu.cn |
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Snippet | The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not completely... Abstract The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not... Abstract The NLRP3 inflammasome plays an important role in protecting the host from infection and aseptic inflammation, and its regulatory mechanism is not... |
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SubjectTerms | Adenosine triphosphate Arthritis Arthritis, Gouty Bacterial infections Cancer Crystals Cytokines Hospitals Humans Infections Infectious diseases Inflammasomes Inflammation Inflammatory diseases Interleukin-1beta Kinases Life sciences NIMA-Related Kinases - genetics NLR Family, Pyrin Domain-Containing 3 Protein - genetics Oligomerization Proteins Therapeutic targets Ubiquitin-protein ligase Uric acid |
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Title | HECTD3 inhibits NLRP3 inflammasome assembly and activation by blocking NLRP3-NEK7 interaction |
URI | https://www.ncbi.nlm.nih.gov/pubmed/38267403 https://www.proquest.com/docview/2918141655/abstract/ https://search.proquest.com/docview/2918511519 https://pubmed.ncbi.nlm.nih.gov/PMC10808187 https://doaj.org/article/8b7cb02cb6e6428aa58c29ecd930264c |
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