Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome
Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane c...
Ausführliche Beschreibung
Autor*in: |
Wenbiao Wang [verfasserIn] Dingwen Hu [verfasserIn] Yuqian Feng [verfasserIn] Caifeng Wu [verfasserIn] Yunting Song [verfasserIn] Weiyong Liu [verfasserIn] Aixin Li [verfasserIn] Yingchong Wang [verfasserIn] Keli Chen [verfasserIn] Mingfu Tian [verfasserIn] Feng Xiao [verfasserIn] Qi Zhang [verfasserIn] Weijie Chen [verfasserIn] Pan Pan [verfasserIn] Pin Wan [verfasserIn] Yingle Liu [verfasserIn] Huiyao Lan [verfasserIn] Kailang Wu [verfasserIn] Jianguo Wu [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Übergeordnetes Werk: |
In: BMC Biology - BMC, 2003, 18(2020), 1, Seite 22 |
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Übergeordnetes Werk: |
volume:18 ; year:2020 ; number:1 ; pages:22 |
Links: |
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DOI / URN: |
10.1186/s12915-020-00918-w |
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Katalog-ID: |
DOAJ017032571 |
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245 | 1 | 0 | |a Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome |
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520 | |a Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. | ||
650 | 4 | |a Adenosine triphosphate, ATP | |
650 | 4 | |a P2X7 receptor | |
650 | 4 | |a Paxillin | |
650 | 4 | |a The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 | |
650 | 4 | |a Ubiquitin-specific peptidase 13, USP13 | |
653 | 0 | |a Biology (General) | |
700 | 0 | |a Dingwen Hu |e verfasserin |4 aut | |
700 | 0 | |a Yuqian Feng |e verfasserin |4 aut | |
700 | 0 | |a Caifeng Wu |e verfasserin |4 aut | |
700 | 0 | |a Yunting Song |e verfasserin |4 aut | |
700 | 0 | |a Weiyong Liu |e verfasserin |4 aut | |
700 | 0 | |a Aixin Li |e verfasserin |4 aut | |
700 | 0 | |a Yingchong Wang |e verfasserin |4 aut | |
700 | 0 | |a Keli Chen |e verfasserin |4 aut | |
700 | 0 | |a Mingfu Tian |e verfasserin |4 aut | |
700 | 0 | |a Feng Xiao |e verfasserin |4 aut | |
700 | 0 | |a Qi Zhang |e verfasserin |4 aut | |
700 | 0 | |a Weijie Chen |e verfasserin |4 aut | |
700 | 0 | |a Pan Pan |e verfasserin |4 aut | |
700 | 0 | |a Pin Wan |e verfasserin |4 aut | |
700 | 0 | |a Yingle Liu |e verfasserin |4 aut | |
700 | 0 | |a Huiyao Lan |e verfasserin |4 aut | |
700 | 0 | |a Kailang Wu |e verfasserin |4 aut | |
700 | 0 | |a Jianguo Wu |e verfasserin |4 aut | |
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10.1186/s12915-020-00918-w doi (DE-627)DOAJ017032571 (DE-599)DOAJ6501c92b4b5045cb996039eebe55494a DE-627 ger DE-627 rakwb eng QH301-705.5 Wenbiao Wang verfasserin aut Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 Biology (General) Dingwen Hu verfasserin aut Yuqian Feng verfasserin aut Caifeng Wu verfasserin aut Yunting Song verfasserin aut Weiyong Liu verfasserin aut Aixin Li verfasserin aut Yingchong Wang verfasserin aut Keli Chen verfasserin aut Mingfu Tian verfasserin aut Feng Xiao verfasserin aut Qi Zhang verfasserin aut Weijie Chen verfasserin aut Pan Pan verfasserin aut Pin Wan verfasserin aut Yingle Liu verfasserin aut Huiyao Lan verfasserin aut Kailang Wu verfasserin aut Jianguo Wu verfasserin aut In BMC Biology BMC, 2003 18(2020), 1, Seite 22 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:18 year:2020 number:1 pages:22 https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/article/6501c92b4b5045cb996039eebe55494a kostenfrei https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 1 22 |
spelling |
10.1186/s12915-020-00918-w doi (DE-627)DOAJ017032571 (DE-599)DOAJ6501c92b4b5045cb996039eebe55494a DE-627 ger DE-627 rakwb eng QH301-705.5 Wenbiao Wang verfasserin aut Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 Biology (General) Dingwen Hu verfasserin aut Yuqian Feng verfasserin aut Caifeng Wu verfasserin aut Yunting Song verfasserin aut Weiyong Liu verfasserin aut Aixin Li verfasserin aut Yingchong Wang verfasserin aut Keli Chen verfasserin aut Mingfu Tian verfasserin aut Feng Xiao verfasserin aut Qi Zhang verfasserin aut Weijie Chen verfasserin aut Pan Pan verfasserin aut Pin Wan verfasserin aut Yingle Liu verfasserin aut Huiyao Lan verfasserin aut Kailang Wu verfasserin aut Jianguo Wu verfasserin aut In BMC Biology BMC, 2003 18(2020), 1, Seite 22 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:18 year:2020 number:1 pages:22 https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/article/6501c92b4b5045cb996039eebe55494a kostenfrei https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 1 22 |
allfields_unstemmed |
10.1186/s12915-020-00918-w doi (DE-627)DOAJ017032571 (DE-599)DOAJ6501c92b4b5045cb996039eebe55494a DE-627 ger DE-627 rakwb eng QH301-705.5 Wenbiao Wang verfasserin aut Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 Biology (General) Dingwen Hu verfasserin aut Yuqian Feng verfasserin aut Caifeng Wu verfasserin aut Yunting Song verfasserin aut Weiyong Liu verfasserin aut Aixin Li verfasserin aut Yingchong Wang verfasserin aut Keli Chen verfasserin aut Mingfu Tian verfasserin aut Feng Xiao verfasserin aut Qi Zhang verfasserin aut Weijie Chen verfasserin aut Pan Pan verfasserin aut Pin Wan verfasserin aut Yingle Liu verfasserin aut Huiyao Lan verfasserin aut Kailang Wu verfasserin aut Jianguo Wu verfasserin aut In BMC Biology BMC, 2003 18(2020), 1, Seite 22 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:18 year:2020 number:1 pages:22 https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/article/6501c92b4b5045cb996039eebe55494a kostenfrei https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 1 22 |
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10.1186/s12915-020-00918-w doi (DE-627)DOAJ017032571 (DE-599)DOAJ6501c92b4b5045cb996039eebe55494a DE-627 ger DE-627 rakwb eng QH301-705.5 Wenbiao Wang verfasserin aut Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 Biology (General) Dingwen Hu verfasserin aut Yuqian Feng verfasserin aut Caifeng Wu verfasserin aut Yunting Song verfasserin aut Weiyong Liu verfasserin aut Aixin Li verfasserin aut Yingchong Wang verfasserin aut Keli Chen verfasserin aut Mingfu Tian verfasserin aut Feng Xiao verfasserin aut Qi Zhang verfasserin aut Weijie Chen verfasserin aut Pan Pan verfasserin aut Pin Wan verfasserin aut Yingle Liu verfasserin aut Huiyao Lan verfasserin aut Kailang Wu verfasserin aut Jianguo Wu verfasserin aut In BMC Biology BMC, 2003 18(2020), 1, Seite 22 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:18 year:2020 number:1 pages:22 https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/article/6501c92b4b5045cb996039eebe55494a kostenfrei https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 1 22 |
allfieldsSound |
10.1186/s12915-020-00918-w doi (DE-627)DOAJ017032571 (DE-599)DOAJ6501c92b4b5045cb996039eebe55494a DE-627 ger DE-627 rakwb eng QH301-705.5 Wenbiao Wang verfasserin aut Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 Biology (General) Dingwen Hu verfasserin aut Yuqian Feng verfasserin aut Caifeng Wu verfasserin aut Yunting Song verfasserin aut Weiyong Liu verfasserin aut Aixin Li verfasserin aut Yingchong Wang verfasserin aut Keli Chen verfasserin aut Mingfu Tian verfasserin aut Feng Xiao verfasserin aut Qi Zhang verfasserin aut Weijie Chen verfasserin aut Pan Pan verfasserin aut Pin Wan verfasserin aut Yingle Liu verfasserin aut Huiyao Lan verfasserin aut Kailang Wu verfasserin aut Jianguo Wu verfasserin aut In BMC Biology BMC, 2003 18(2020), 1, Seite 22 (DE-627)377757241 (DE-600)2133020-7 17417007 nnns volume:18 year:2020 number:1 pages:22 https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/article/6501c92b4b5045cb996039eebe55494a kostenfrei https://doi.org/10.1186/s12915-020-00918-w kostenfrei https://doaj.org/toc/1741-7007 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 1 22 |
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Wenbiao Wang @@aut@@ Dingwen Hu @@aut@@ Yuqian Feng @@aut@@ Caifeng Wu @@aut@@ Yunting Song @@aut@@ Weiyong Liu @@aut@@ Aixin Li @@aut@@ Yingchong Wang @@aut@@ Keli Chen @@aut@@ Mingfu Tian @@aut@@ Feng Xiao @@aut@@ Qi Zhang @@aut@@ Weijie Chen @@aut@@ Pan Pan @@aut@@ Pin Wan @@aut@@ Yingle Liu @@aut@@ Huiyao Lan @@aut@@ Kailang Wu @@aut@@ Jianguo Wu @@aut@@ |
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ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. 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Wenbiao Wang |
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QH301-705.5 Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome Adenosine triphosphate, ATP P2X7 receptor Paxillin The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 Ubiquitin-specific peptidase 13, USP13 |
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misc QH301-705.5 misc Adenosine triphosphate, ATP misc P2X7 receptor misc Paxillin misc The NACHT, LRR, and PYD domain-containing protein 3, NLRP3 misc Ubiquitin-specific peptidase 13, USP13 misc Biology (General) |
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Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome |
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Wenbiao Wang Dingwen Hu Yuqian Feng Caifeng Wu Yunting Song Weiyong Liu Aixin Li Yingchong Wang Keli Chen Mingfu Tian Feng Xiao Qi Zhang Weijie Chen Pan Pan Pin Wan Yingle Liu Huiyao Lan Kailang Wu Jianguo Wu |
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paxillin mediates atp-induced activation of p2x7 receptor and nlrp3 inflammasome |
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Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome |
abstract |
Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. |
abstractGer |
Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. |
abstract_unstemmed |
Abstract Background Extracellular adenosine triphosphate (ATP), a key danger-associated molecular pattern (DAMP) molecule, is released to the extracellular medium during inflammation by injured parenchymal cells, dying leukocytes, and activated platelets. ATP directly activates the plasma membrane channel P2X7 receptor (P2X7R), leading to an intracellular influx of K+, a key trigger inducing NLRP3 inflammasome activation. However, the mechanism underlying P2X7R-mediated activation of NLRP3 inflammasome is poorly understood, and additional molecular mediators have not been identified. Here, we demonstrate that Paxillin is the molecule connecting the P2X7 receptor and NLRP3 inflammasome through protein interactions. Results We show a distinct mechanism by which Paxillin promotes ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome. Extracellular ATP induces Paxillin phosphorylation and then facilitates Paxillin-NLRP3 interaction. Interestingly, Paxillin enhances NLRP3 deubiquitination and activates NLRP3 inflammasome upon ATP treatment and K+ efflux. Moreover, we demonstrated that USP13 is a key enzyme for Paxillin-mediated NLRP3 deubiquitination upon ATP treatment. Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. Paxillin plays key roles in ATP-induced activation of the P2X7 receptor and NLRP3 inflammasome by facilitating the formation of the P2X7R-Paxillin-NLRP3 complex. |
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Paxillin mediates ATP-induced activation of P2X7 receptor and NLRP3 inflammasome |
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https://doi.org/10.1186/s12915-020-00918-w https://doaj.org/article/6501c92b4b5045cb996039eebe55494a https://doaj.org/toc/1741-7007 |
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Dingwen Hu Yuqian Feng Caifeng Wu Yunting Song Weiyong Liu Aixin Li Yingchong Wang Keli Chen Mingfu Tian Feng Xiao Qi Zhang Weijie Chen Pan Pan Pin Wan Yingle Liu Huiyao Lan Kailang Wu Jianguo Wu |
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Dingwen Hu Yuqian Feng Caifeng Wu Yunting Song Weiyong Liu Aixin Li Yingchong Wang Keli Chen Mingfu Tian Feng Xiao Qi Zhang Weijie Chen Pan Pan Pin Wan Yingle Liu Huiyao Lan Kailang Wu Jianguo Wu |
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Notably, extracellular ATP promotes Paxillin and NLRP3 migration from the cytosol to the plasma membrane and facilitates P2X7R-Paxillin interaction and PaxillinNLRP3 association, resulting in the formation of the P2X7R-Paxillin-NLRP3 complex. Functionally, Paxillin is essential for ATP-induced NLRP3 inflammasome activation in mouse BMDMs and BMDCs as well as in human PBMCs and THP-1-differentiated macrophages. Conclusions We have identified paxillin as a mediator of NLRP3 inflammasome activation. 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