SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response
As a canonical adaptor for the Toll-like receptor (TLR) family, myeloid differentiation primary response protein 88 (MyD88) has crucial roles in host defense against infection by microbial pathogens, and its dysregulation might induce autoimmune diseases. Here, we demonstrate that the chicken Cullin...
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| Veröffentlicht in: | PLoS pathogens 2020-05, Vol.16 (5), p.e1008188-e1008188 |
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| creator | Li, Qinghe Wang, Fei Wang, Qiao Zhang, Na Zheng, Jumei Zheng, Maiqing Liu, Ranran Cui, Huanxian Wen, Jie Zhao, Guiping |
| description | As a canonical adaptor for the Toll-like receptor (TLR) family, myeloid differentiation primary response protein 88 (MyD88) has crucial roles in host defense against infection by microbial pathogens, and its dysregulation might induce autoimmune diseases. Here, we demonstrate that the chicken Cullin 3-based ubiquitin ligase adaptor Speckle-type BTB-POZ protein (chSPOP) recognizes the intermediate domain of chicken MyD88 (chMyD88) and degrades it through the proteasome pathway. Knockdown or genetic ablation of chSPOP leads to aberrant elevation of chMyD88 protein. Through this interaction, chSPOP negatively regulates NF-κB pathway activity and thus the production of IL-1β upon LPS challenge in chicken macrophages. Furthermore, Spop-deficient mice are more susceptible to infection with Salmonella typhimurium. Collectively, these findings demonstrate MyD88 as a bona fide substrate of SPOP and uncover a mechanism by which SPOP regulates MyD88 abundance and disease susceptibility. |
| doi_str_mv | 10.1371/journal.ppat.1008188 |
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Here, we demonstrate that the chicken Cullin 3-based ubiquitin ligase adaptor Speckle-type BTB-POZ protein (chSPOP) recognizes the intermediate domain of chicken MyD88 (chMyD88) and degrades it through the proteasome pathway. Knockdown or genetic ablation of chSPOP leads to aberrant elevation of chMyD88 protein. Through this interaction, chSPOP negatively regulates NF-κB pathway activity and thus the production of IL-1β upon LPS challenge in chicken macrophages. Furthermore, Spop-deficient mice are more susceptible to infection with Salmonella typhimurium. Collectively, these findings demonstrate MyD88 as a bona fide substrate of SPOP and uncover a mechanism by which SPOP regulates MyD88 abundance and disease susceptibility.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1008188</identifier><identifier>PMID: 32365080</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Ablation ; Animal sciences ; Antibodies ; Autoimmune diseases ; Biology and Life Sciences ; Chickens ; Cullin ; Cytokines ; Funding ; Health aspects ; Host-parasite relationships ; IL-1β ; Immune response ; Immune system ; Infections ; Innate immunity ; Kinases ; Laboratories ; Lipopolysaccharides ; Macrophages ; Medicine and Health Sciences ; Microorganisms ; Mutation ; MyD88 protein ; NF-κB protein ; Nutrition ; Observations ; Pathogens ; Phosphatase ; Phosphorylation ; Poultry ; Proteasomes ; Proteins ; Regulation ; Research and Analysis Methods ; Salmonella ; Substrates ; Toll-like receptors ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitination</subject><ispartof>PLoS pathogens, 2020-05, Vol.16 (5), p.e1008188-e1008188</ispartof><rights>COPYRIGHT 2020 Public Library of Science</rights><rights>2020 Li et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2020 Li et al 2020 Li et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c661t-14f88bc0dff5796fca19eb4a69115c1cbca327c15c603195dfcc114586290bf53</citedby><cites>FETCH-LOGICAL-c661t-14f88bc0dff5796fca19eb4a69115c1cbca327c15c603195dfcc114586290bf53</cites><orcidid>0000-0002-9698-829X ; 0000-0003-1332-3952</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7224567/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7224567/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32365080$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Luo, Zhao-Qing</contributor><creatorcontrib>Li, Qinghe</creatorcontrib><creatorcontrib>Wang, Fei</creatorcontrib><creatorcontrib>Wang, Qiao</creatorcontrib><creatorcontrib>Zhang, Na</creatorcontrib><creatorcontrib>Zheng, Jumei</creatorcontrib><creatorcontrib>Zheng, Maiqing</creatorcontrib><creatorcontrib>Liu, Ranran</creatorcontrib><creatorcontrib>Cui, Huanxian</creatorcontrib><creatorcontrib>Wen, Jie</creatorcontrib><creatorcontrib>Zhao, Guiping</creatorcontrib><title>SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response</title><title>PLoS pathogens</title><addtitle>PLoS Pathog</addtitle><description>As a canonical adaptor for the Toll-like receptor (TLR) family, myeloid differentiation primary response protein 88 (MyD88) has crucial roles in host defense against infection by microbial pathogens, and its dysregulation might induce autoimmune diseases. Here, we demonstrate that the chicken Cullin 3-based ubiquitin ligase adaptor Speckle-type BTB-POZ protein (chSPOP) recognizes the intermediate domain of chicken MyD88 (chMyD88) and degrades it through the proteasome pathway. Knockdown or genetic ablation of chSPOP leads to aberrant elevation of chMyD88 protein. Through this interaction, chSPOP negatively regulates NF-κB pathway activity and thus the production of IL-1β upon LPS challenge in chicken macrophages. Furthermore, Spop-deficient mice are more susceptible to infection with Salmonella typhimurium. Collectively, these findings demonstrate MyD88 as a bona fide substrate of SPOP and uncover a mechanism by which SPOP regulates MyD88 abundance and disease susceptibility.</description><subject>Ablation</subject><subject>Animal sciences</subject><subject>Antibodies</subject><subject>Autoimmune diseases</subject><subject>Biology and Life Sciences</subject><subject>Chickens</subject><subject>Cullin</subject><subject>Cytokines</subject><subject>Funding</subject><subject>Health aspects</subject><subject>Host-parasite relationships</subject><subject>IL-1β</subject><subject>Immune response</subject><subject>Immune system</subject><subject>Infections</subject><subject>Innate immunity</subject><subject>Kinases</subject><subject>Laboratories</subject><subject>Lipopolysaccharides</subject><subject>Macrophages</subject><subject>Medicine and Health Sciences</subject><subject>Microorganisms</subject><subject>Mutation</subject><subject>MyD88 protein</subject><subject>NF-κB protein</subject><subject>Nutrition</subject><subject>Observations</subject><subject>Pathogens</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>Poultry</subject><subject>Proteasomes</subject><subject>Proteins</subject><subject>Regulation</subject><subject>Research and Analysis Methods</subject><subject>Salmonella</subject><subject>Substrates</subject><subject>Toll-like receptors</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein 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ubiquitination and degradation of MyD88 to suppress the innate immune response</title><author>Li, Qinghe ; Wang, Fei ; Wang, Qiao ; Zhang, Na ; Zheng, Jumei ; Zheng, Maiqing ; Liu, Ranran ; Cui, Huanxian ; Wen, Jie ; Zhao, Guiping</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c661t-14f88bc0dff5796fca19eb4a69115c1cbca327c15c603195dfcc114586290bf53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Ablation</topic><topic>Animal sciences</topic><topic>Antibodies</topic><topic>Autoimmune diseases</topic><topic>Biology and Life Sciences</topic><topic>Chickens</topic><topic>Cullin</topic><topic>Cytokines</topic><topic>Funding</topic><topic>Health aspects</topic><topic>Host-parasite relationships</topic><topic>IL-1β</topic><topic>Immune response</topic><topic>Immune system</topic><topic>Infections</topic><topic>Innate immunity</topic><topic>Kinases</topic><topic>Laboratories</topic><topic>Lipopolysaccharides</topic><topic>Macrophages</topic><topic>Medicine and Health Sciences</topic><topic>Microorganisms</topic><topic>Mutation</topic><topic>MyD88 protein</topic><topic>NF-κB protein</topic><topic>Nutrition</topic><topic>Observations</topic><topic>Pathogens</topic><topic>Phosphatase</topic><topic>Phosphorylation</topic><topic>Poultry</topic><topic>Proteasomes</topic><topic>Proteins</topic><topic>Regulation</topic><topic>Research and Analysis Methods</topic><topic>Salmonella</topic><topic>Substrates</topic><topic>Toll-like receptors</topic><topic>Ubiquitin</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Qinghe</creatorcontrib><creatorcontrib>Wang, Fei</creatorcontrib><creatorcontrib>Wang, Qiao</creatorcontrib><creatorcontrib>Zhang, Na</creatorcontrib><creatorcontrib>Zheng, 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Zhao-Qing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2020-05-01</date><risdate>2020</risdate><volume>16</volume><issue>5</issue><spage>e1008188</spage><epage>e1008188</epage><pages>e1008188-e1008188</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>As a canonical adaptor for the Toll-like receptor (TLR) family, myeloid differentiation primary response protein 88 (MyD88) has crucial roles in host defense against infection by microbial pathogens, and its dysregulation might induce autoimmune diseases. Here, we demonstrate that the chicken Cullin 3-based ubiquitin ligase adaptor Speckle-type BTB-POZ protein (chSPOP) recognizes the intermediate domain of chicken MyD88 (chMyD88) and degrades it through the proteasome pathway. Knockdown or genetic ablation of chSPOP leads to aberrant elevation of chMyD88 protein. Through this interaction, chSPOP negatively regulates NF-κB pathway activity and thus the production of IL-1β upon LPS challenge in chicken macrophages. Furthermore, Spop-deficient mice are more susceptible to infection with Salmonella typhimurium. Collectively, these findings demonstrate MyD88 as a bona fide substrate of SPOP and uncover a mechanism by which SPOP regulates MyD88 abundance and disease susceptibility.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>32365080</pmid><doi>10.1371/journal.ppat.1008188</doi><orcidid>https://orcid.org/0000-0002-9698-829X</orcidid><orcidid>https://orcid.org/0000-0003-1332-3952</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Ablation Animal sciences Antibodies Autoimmune diseases Biology and Life Sciences Chickens Cullin Cytokines Funding Health aspects Host-parasite relationships IL-1β Immune response Immune system Infections Innate immunity Kinases Laboratories Lipopolysaccharides Macrophages Medicine and Health Sciences Microorganisms Mutation MyD88 protein NF-κB protein Nutrition Observations Pathogens Phosphatase Phosphorylation Poultry Proteasomes Proteins Regulation Research and Analysis Methods Salmonella Substrates Toll-like receptors Ubiquitin Ubiquitin-protein ligase Ubiquitination |
| title | SPOP promotes ubiquitination and degradation of MyD88 to suppress the innate immune response |
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