Pathogen blockade of TAK1 triggers caspase-8-dependent cleavage of gasdermin D and cell death

Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe a...

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Vydáno v:	Science (American Association for the Advancement of Science) Ročník 362; číslo 6418; s. 1064
Hlavní autoři:	Orning, Pontus, Weng, Dan, Starheim, Kristian, Ratner, Dmitry, Best, Zachary, Lee, Bettina, Brooks, Alexandria, Xia, Shiyu, Wu, Hao, Kelliher, Michelle A, Berger, Scott B, Gough, Peter J, Bertin, John, Proulx, Megan M, Goguen, Jon D, Kayagaki, Nobuhiko, Fitzgerald, Katherine A, Lien, Egil
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 30.11.2018
Témata:	Animals Apoptosis Regulatory Proteins - metabolism Bacterial Proteins - metabolism Caspase 8 - genetics Caspase 8 - metabolism Cell Death Host-Pathogen Interactions Humans I-kappa B Kinase - metabolism Inflammasomes - immunology MAP Kinase Kinase Kinases - metabolism Mice Mice, Inbred C57BL NLR Family, Pyrin Domain-Containing 3 Protein Plague - enzymology Plague - immunology Plague - pathology Proteolysis
ISSN:	1095-9203, 1095-9203
On-line přístup:	Zjistit podrobnosti o přístupu
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Abstract	Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe an additional pathway controlling GSDMD processing. The inhibition of TAK1 or IκB kinase (IKK) by the effector protein YopJ elicits RIPK1- and caspase-8-dependent cleavage of GSDMD, which subsequently results in cell death. GSDMD processing also contributes to the NLRP3 inflammasome-dependent release of interleukin-1β (IL-1β). Thus, caspase-8 acts as a regulator of GSDMD-driven cell death. Furthermore, this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity.
AbstractList	Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe an additional pathway controlling GSDMD processing. The inhibition of TAK1 or IκB kinase (IKK) by the effector protein YopJ elicits RIPK1- and caspase-8-dependent cleavage of GSDMD, which subsequently results in cell death. GSDMD processing also contributes to the NLRP3 inflammasome-dependent release of interleukin-1β (IL-1β). Thus, caspase-8 acts as a regulator of GSDMD-driven cell death. Furthermore, this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity. Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe an additional pathway controlling GSDMD processing. The inhibition of TAK1 or IκB kinase (IKK) by the Yersinia effector protein YopJ elicits RIPK1- and caspase-8-dependent cleavage of GSDMD, which subsequently results in cell death. GSDMD processing also contributes to the NLRP3 inflammasome-dependent release of interleukin-1β (IL-1β). Thus, caspase-8 acts as a regulator of GSDMD-driven cell death. Furthermore, this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity.Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via inflammasome-activated caspase-1 or -11. It is currently unknown whether macrophage GSDMD can be processed by other mechanisms. Here, we describe an additional pathway controlling GSDMD processing. The inhibition of TAK1 or IκB kinase (IKK) by the Yersinia effector protein YopJ elicits RIPK1- and caspase-8-dependent cleavage of GSDMD, which subsequently results in cell death. GSDMD processing also contributes to the NLRP3 inflammasome-dependent release of interleukin-1β (IL-1β). Thus, caspase-8 acts as a regulator of GSDMD-driven cell death. Furthermore, this study establishes the importance of TAK1 and IKK activity in the control of GSDMD cleavage and cytotoxicity.
Author	Best, Zachary Lien, Egil Wu, Hao Brooks, Alexandria Berger, Scott B Bertin, John Gough, Peter J Starheim, Kristian Weng, Dan Kayagaki, Nobuhiko Kelliher, Michelle A Ratner, Dmitry Proulx, Megan M Orning, Pontus Goguen, Jon D Fitzgerald, Katherine A Lee, Bettina Xia, Shiyu
Author_xml	– sequence: 1 givenname: Pontus orcidid: 0000-0002-6177-6916 surname: Orning fullname: Orning, Pontus organization: Centre of Molecular Inflammation Research, Department of Clinical and Molecular Medicine, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 2 givenname: Dan surname: Weng fullname: Weng, Dan organization: Center for Molecular Metabolism, Nanjing University of Science and Technology, Nanjing 210094, China – sequence: 3 givenname: Kristian surname: Starheim fullname: Starheim, Kristian organization: Centre of Molecular Inflammation Research, Department of Clinical and Molecular Medicine, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 4 givenname: Dmitry orcidid: 0000-0002-1706-2596 surname: Ratner fullname: Ratner, Dmitry organization: Program in Innate Immunity, Department of Medicine, Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 5 givenname: Zachary orcidid: 0000-0002-8645-6441 surname: Best fullname: Best, Zachary organization: Program in Innate Immunity, Department of Medicine, Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 6 givenname: Bettina surname: Lee fullname: Lee, Bettina organization: Department of Physiological Chemistry, Genentech, South San Francisco, CA 94080, USA – sequence: 7 givenname: Alexandria orcidid: 0000-0002-1119-2568 surname: Brooks fullname: Brooks, Alexandria organization: Program in Innate Immunity, Department of Medicine, Division of Infectious Diseases and Immunology, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 8 givenname: Shiyu surname: Xia fullname: Xia, Shiyu organization: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA – sequence: 9 givenname: Hao orcidid: 0000-0002-7281-8579 surname: Wu fullname: Wu, Hao organization: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, and Program in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA 02115, USA – sequence: 10 givenname: Michelle A orcidid: 0000-0001-9211-3659 surname: Kelliher fullname: Kelliher, Michelle A organization: Department of Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 11 givenname: Scott B surname: Berger fullname: Berger, Scott B organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-inflammation Therapeutic Area, GlaxoSmithKline, Collegeville, PA 19426, USA – sequence: 12 givenname: Peter J orcidid: 0000-0002-5110-9300 surname: Gough fullname: Gough, Peter J organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-inflammation Therapeutic Area, GlaxoSmithKline, Collegeville, PA 19426, USA – sequence: 13 givenname: John surname: Bertin fullname: Bertin, John organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-inflammation Therapeutic Area, GlaxoSmithKline, Collegeville, PA 19426, USA – sequence: 14 givenname: Megan M orcidid: 0000-0002-9524-8302 surname: Proulx fullname: Proulx, Megan M organization: Department of Microbiology and Physiology, University of Massachusetts Medical School, Worcester, MA 01655, USA – sequence: 15 givenname: Jon D surname: Goguen fullname: Goguen, Jon D organization: Department of Microbiology and Physiology, University of Massachusetts Medical School, Worcester, MA 01655, USA – sequence: 16 givenname: Nobuhiko surname: Kayagaki fullname: Kayagaki, Nobuhiko organization: Department of Physiological Chemistry, Genentech, South San Francisco, CA 94080, USA – sequence: 17 givenname: Katherine A surname: Fitzgerald fullname: Fitzgerald, Katherine A organization: Centre of Molecular Inflammation Research, Department of Clinical and Molecular Medicine, Norwegian University of Science and Technology, 7491 Trondheim, Norway – sequence: 18 givenname: Egil orcidid: 0000-0002-8536-2419 surname: Lien fullname: Lien, Egil email: egil.lien@umassmed.edu organization: Centre of Molecular Inflammation Research, Department of Clinical and Molecular Medicine, Norwegian University of Science and Technology, 7491 Trondheim, Norway
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Snippet	Limited proteolysis of gasdermin D (GSDMD) generates an N-terminal pore-forming fragment that controls pyroptosis in macrophages. GSDMD is processed via...
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SubjectTerms	Animals Apoptosis Regulatory Proteins - metabolism Bacterial Proteins - metabolism Caspase 8 - genetics Caspase 8 - metabolism Cell Death Host-Pathogen Interactions Humans I-kappa B Kinase - metabolism Inflammasomes - immunology MAP Kinase Kinase Kinases - metabolism Mice Mice, Inbred C57BL NLR Family, Pyrin Domain-Containing 3 Protein Plague - enzymology Plague - immunology Plague - pathology Proteolysis
Title	Pathogen blockade of TAK1 triggers caspase-8-dependent cleavage of gasdermin D and cell death
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