LRRFIP2 negatively regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I-mediated caspase-1 inhibition
The NLRP3 inflammasome is the most characterized inflammasome activated by cellular infection or stress, which is responsible for the maturation of proinflammatory cytokines IL-1β and IL-18. The precise molecular mechanism for negative regulation of NLRP3 inflammasome activation needs to be further...
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| Veröffentlicht in: | Nature communications 2013-08, Vol.4 (1), p.2075-2075, Article 2075 |
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| creator | Jin, Jing Yu, Qian Han, Chaofeng Hu, Xiang Xu, Sheng Wang, Qingqing Wang, Jianli Li, Nan Cao, Xuetao |
| description | The NLRP3 inflammasome is the most characterized inflammasome activated by cellular infection or stress, which is responsible for the maturation of proinflammatory cytokines IL-1β and IL-18. The precise molecular mechanism for negative regulation of NLRP3 inflammasome activation needs to be further defined. Here we identify leucine-rich repeat Fli-I-interacting protein 2 (LRRFIP2) as an NLRP3-associated protein and an inhibitor for NLRP3 inflammasome activation. LRRFIP2 binds to NLRP3 via its N terminus upon NLRP3 inflammasome activation, and also interacts with Flightless-I, a pseudosubstrate of caspase-1, via its Coil motif. Knockdown of Flightless-I significantly promotes NLRP3 inflammasome activation. LRRFIP2 enhances the interaction between Flightless-I and caspase-1, facilitating the inhibitory effect of Flightless-I on caspase-1 activation. Furthermore, silencing of Flightless-I abrogates the inhibitory effect of LRRFIP2 on NLRP3 inflammasome. These data demonstrate that LRRFIP2 inhibits NLRP3 inflammasome activation by recruiting the caspase-1 inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 inflammasome.
Inflammasomes promote the maturation of inflammatory cytokines in response to signals associated with damage and infection, but it remains unclear how these signals are attenuated. Here, the authors show that the NLRP3 inflammasome is inhibited by LRRFIP2 through recruitment of the protein Flightless I. |
| doi_str_mv | 10.1038/ncomms3075 |
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Inflammasomes promote the maturation of inflammatory cytokines in response to signals associated with damage and infection, but it remains unclear how these signals are attenuated. Here, the authors show that the NLRP3 inflammasome is inhibited by LRRFIP2 through recruitment of the protein Flightless I.</description><identifier>ISSN: 2041-1723</identifier><identifier>EISSN: 2041-1723</identifier><identifier>DOI: 10.1038/ncomms3075</identifier><identifier>PMID: 23942110</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/250/2504/342 ; 631/250/256/2177 ; 631/250/262/2106/2517 ; 631/250/516 ; Animals ; Carrier Proteins - biosynthesis ; Carrier Proteins - metabolism ; Caspase 1 - metabolism ; Caspase Inhibitors ; Cells, Cultured ; Cytoskeletal Proteins - genetics ; Cytoskeletal Proteins - metabolism ; Enzyme Activation ; Female ; Humanities and Social Sciences ; Inflammasomes - biosynthesis ; Inflammasomes - metabolism ; Macrophages - metabolism ; Mice ; Mice, Inbred C57BL ; multidisciplinary ; NLR Family, Pyrin Domain-Containing 3 Protein ; Peritonitis ; RNA Interference ; RNA, Small Interfering ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Science ; Science (multidisciplinary)</subject><ispartof>Nature communications, 2013-08, Vol.4 (1), p.2075-2075, Article 2075</ispartof><rights>The Author(s) 2013</rights><rights>Copyright Nature Publishing Group Aug 2013</rights><rights>Copyright © 2013, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-e175afe23d0bb1ec23a9ac3eee0a4dbf41bb0a85112e64b71463ec5c36d7e88e3</citedby><cites>FETCH-LOGICAL-c508t-e175afe23d0bb1ec23a9ac3eee0a4dbf41bb0a85112e64b71463ec5c36d7e88e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753543/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753543/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23942110$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jin, Jing</creatorcontrib><creatorcontrib>Yu, Qian</creatorcontrib><creatorcontrib>Han, Chaofeng</creatorcontrib><creatorcontrib>Hu, Xiang</creatorcontrib><creatorcontrib>Xu, Sheng</creatorcontrib><creatorcontrib>Wang, Qingqing</creatorcontrib><creatorcontrib>Wang, Jianli</creatorcontrib><creatorcontrib>Li, Nan</creatorcontrib><creatorcontrib>Cao, Xuetao</creatorcontrib><title>LRRFIP2 negatively regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I-mediated caspase-1 inhibition</title><title>Nature communications</title><addtitle>Nat Commun</addtitle><addtitle>Nat Commun</addtitle><description>The NLRP3 inflammasome is the most characterized inflammasome activated by cellular infection or stress, which is responsible for the maturation of proinflammatory cytokines IL-1β and IL-18. The precise molecular mechanism for negative regulation of NLRP3 inflammasome activation needs to be further defined. Here we identify leucine-rich repeat Fli-I-interacting protein 2 (LRRFIP2) as an NLRP3-associated protein and an inhibitor for NLRP3 inflammasome activation. LRRFIP2 binds to NLRP3 via its N terminus upon NLRP3 inflammasome activation, and also interacts with Flightless-I, a pseudosubstrate of caspase-1, via its Coil motif. Knockdown of Flightless-I significantly promotes NLRP3 inflammasome activation. LRRFIP2 enhances the interaction between Flightless-I and caspase-1, facilitating the inhibitory effect of Flightless-I on caspase-1 activation. Furthermore, silencing of Flightless-I abrogates the inhibitory effect of LRRFIP2 on NLRP3 inflammasome. These data demonstrate that LRRFIP2 inhibits NLRP3 inflammasome activation by recruiting the caspase-1 inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 inflammasome.
Inflammasomes promote the maturation of inflammatory cytokines in response to signals associated with damage and infection, but it remains unclear how these signals are attenuated. Here, the authors show that the NLRP3 inflammasome is inhibited by LRRFIP2 through recruitment of the protein Flightless I.</description><subject>631/250/2504/342</subject><subject>631/250/256/2177</subject><subject>631/250/262/2106/2517</subject><subject>631/250/516</subject><subject>Animals</subject><subject>Carrier Proteins - biosynthesis</subject><subject>Carrier Proteins - metabolism</subject><subject>Caspase 1 - metabolism</subject><subject>Caspase Inhibitors</subject><subject>Cells, Cultured</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Enzyme Activation</subject><subject>Female</subject><subject>Humanities and Social Sciences</subject><subject>Inflammasomes - biosynthesis</subject><subject>Inflammasomes - metabolism</subject><subject>Macrophages - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>multidisciplinary</subject><subject>NLR Family, Pyrin Domain-Containing 3 Protein</subject><subject>Peritonitis</subject><subject>RNA Interference</subject><subject>RNA, Small Interfering</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>2041-1723</issn><issn>2041-1723</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkV1rFDEUhgdRbKm98QfIgDeijOZzZ_ZGkOLahUXLotfhJHNmNmWSjMlMYS_952bZ2q6am4ScJ0_e5BTFS0reU8KbD94E5xIntXxSnDMiaEVrxp-erM-Ky5RuSR58SRshnhdnjC8Fo5ScF7822-1qfcNKjz1M9g6HfRmxnweYMJVfN9sbXlrfDeAcpOCwBJOpTAaf90sHJoZxB32G9b4cY3Bhsr4vV4Ptd9OAKVXrymFrs68tDaQRElY0n91ZbQ-aF8WzDoaEl_fzRfFj9fn71XW1-fZlffVpUxlJmqlCWkvokPGWaE3RMA5LMBwRCYhWd4JqTaCRlDJcCF1TseBopOGLtsamQX5RfDx6x1nnQAb9FGFQY7QO4l4FsOrvirc71Yc7xWvJpeBZ8OZeEMPPGdOknE0GhwE8hjkpKpjgTAp5QF__g96GOfr8vANFaN3IpcjU2yOV_zCliN1DGErUobnqsbkZfnUa_wH908oMvDsCKZd8j_Hkzv91vwELjrI5</recordid><startdate>20130814</startdate><enddate>20130814</enddate><creator>Jin, Jing</creator><creator>Yu, Qian</creator><creator>Han, Chaofeng</creator><creator>Hu, Xiang</creator><creator>Xu, Sheng</creator><creator>Wang, Qingqing</creator><creator>Wang, Jianli</creator><creator>Li, Nan</creator><creator>Cao, Xuetao</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><general>Nature Pub. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jin, Jing</au><au>Yu, Qian</au><au>Han, Chaofeng</au><au>Hu, Xiang</au><au>Xu, Sheng</au><au>Wang, Qingqing</au><au>Wang, Jianli</au><au>Li, Nan</au><au>Cao, Xuetao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>LRRFIP2 negatively regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I-mediated caspase-1 inhibition</atitle><jtitle>Nature communications</jtitle><stitle>Nat Commun</stitle><addtitle>Nat Commun</addtitle><date>2013-08-14</date><risdate>2013</risdate><volume>4</volume><issue>1</issue><spage>2075</spage><epage>2075</epage><pages>2075-2075</pages><artnum>2075</artnum><issn>2041-1723</issn><eissn>2041-1723</eissn><abstract>The NLRP3 inflammasome is the most characterized inflammasome activated by cellular infection or stress, which is responsible for the maturation of proinflammatory cytokines IL-1β and IL-18. The precise molecular mechanism for negative regulation of NLRP3 inflammasome activation needs to be further defined. Here we identify leucine-rich repeat Fli-I-interacting protein 2 (LRRFIP2) as an NLRP3-associated protein and an inhibitor for NLRP3 inflammasome activation. LRRFIP2 binds to NLRP3 via its N terminus upon NLRP3 inflammasome activation, and also interacts with Flightless-I, a pseudosubstrate of caspase-1, via its Coil motif. Knockdown of Flightless-I significantly promotes NLRP3 inflammasome activation. LRRFIP2 enhances the interaction between Flightless-I and caspase-1, facilitating the inhibitory effect of Flightless-I on caspase-1 activation. Furthermore, silencing of Flightless-I abrogates the inhibitory effect of LRRFIP2 on NLRP3 inflammasome. These data demonstrate that LRRFIP2 inhibits NLRP3 inflammasome activation by recruiting the caspase-1 inhibitor Flightless-I, thus outlining a new mechanism for negative regulation of NLRP3 inflammasome.
Inflammasomes promote the maturation of inflammatory cytokines in response to signals associated with damage and infection, but it remains unclear how these signals are attenuated. Here, the authors show that the NLRP3 inflammasome is inhibited by LRRFIP2 through recruitment of the protein Flightless I.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23942110</pmid><doi>10.1038/ncomms3075</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/250/2504/342 631/250/256/2177 631/250/262/2106/2517 631/250/516 Animals Carrier Proteins - biosynthesis Carrier Proteins - metabolism Caspase 1 - metabolism Caspase Inhibitors Cells, Cultured Cytoskeletal Proteins - genetics Cytoskeletal Proteins - metabolism Enzyme Activation Female Humanities and Social Sciences Inflammasomes - biosynthesis Inflammasomes - metabolism Macrophages - metabolism Mice Mice, Inbred C57BL multidisciplinary NLR Family, Pyrin Domain-Containing 3 Protein Peritonitis RNA Interference RNA, Small Interfering RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Science Science (multidisciplinary) |
| title | LRRFIP2 negatively regulates NLRP3 inflammasome activation in macrophages by promoting Flightless-I-mediated caspase-1 inhibition |
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