Protein kinase D at the Golgi controls NLRP3 inflammasome activation

The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP...

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Published inThe Journal of experimental medicine Vol. 214; no. 9; pp. 2671 - 2693
Main Authors Zhang, Zhirong, Meszaros, Gergö, He, Wan-ting, Xu, Yanfang, de Fatima Magliarelli, Helena, Mailly, Laurent, Mihlan, Michael, Liu, Yansheng, Puig Gámez, Marta, Goginashvili, Alexander, Pasquier, Adrien, Bielska, Olga, Neven, Bénédicte, Quartier, Pierre, Aebersold, Rudolf, Baumert, Thomas F., Georgel, Philippe, Han, Jiahuai, Ricci, Romeo
Format Journal Article
LanguageEnglish
Published United States Rockefeller University Press 04.09.2017
The Rockefeller University Press
Subjects
Activation
Animals
Assembly
Cytosol
Deactivation
Diglycerides
Diglycerides - metabolism
Endoplasmic reticulum
Endoplasmic Reticulum - physiology
Golgi apparatus
Golgi Apparatus - physiology
Hazards
Humans
Immune response
Inactivation
Inflammasomes
Inflammasomes - physiology
Innate immunity
Kinases
Leukocytes (mononuclear)
Leukocytes, Mononuclear - metabolism
Membranes
Mice
Mice, Inbred C57BL
Mice, Knockout
Mitochondria
Mutation
NLR Family, Pyrin Domain-Containing 3 Protein - physiology
Oligomerization
Peripheral blood mononuclear cells
Phosphorylation
Protein kinase
Protein Kinase C - physiology
Proteins
Signaling
Online AccessGet full text

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Abstract The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
AbstractList The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
Zhang et al. show that Golgi-mediated protein kinase D (PKD) signaling is required and sufficient for NLRP3 inflammasome activation. PKD at the Golgi phosphorylates NLRP3 to release it from mitochondria-associated endoplasmic reticulum membranes, allowing for assembly of the mature inflammasome in the cytosol. The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
Zhang et al. show that Golgi-mediated protein kinase D (PKD) signaling is required and sufficient for NLRP3 inflammasome activation. PKD at the Golgi phosphorylates NLRP3 to release it from mitochondria-associated endoplasmic reticulum membranes, allowing for assembly of the mature inflammasome in the cytosol.The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes containing distinct sensor molecules exist. The NLRP3 inflammasome is unique as it detects a variety of danger signals. It has been reported that NLRP3 is recruited to mitochondria-associated endoplasmic reticulum membranes (MAMs) and is activated by MAM-derived effectors. Here, we show that in response to inflammasome activators, MAMs localize adjacent to Golgi membranes. Diacylglycerol (DAG) at the Golgi rapidly increases, recruiting protein kinase D (PKD), a key effector of DAG. Upon PKD inactivation, self-oligomerized NLRP3 is retained at MAMs adjacent to Golgi, blocking assembly of the active inflammasome. Importantly, phosphorylation of NLRP3 by PKD at the Golgi is sufficient to release NLRP3 from MAMs, resulting in assembly of the active inflammasome. Moreover, PKD inhibition prevents inflammasome autoactivation in peripheral blood mononuclear cells from patients carrying NLRP3 mutations. Hence, Golgi-mediated PKD signaling is required and sufficient for NLRP3 inflammasome activation.
Author Puig Gámez, Marta
Neven, Bénédicte
Meszaros, Gergö
Quartier, Pierre
Georgel, Philippe
Goginashvili, Alexander
Ricci, Romeo
Aebersold, Rudolf
Xu, Yanfang
He, Wan-ting
Zhang, Zhirong
de Fatima Magliarelli, Helena
Baumert, Thomas F.
Mihlan, Michael
Bielska, Olga
Mailly, Laurent
Han, Jiahuai
Liu, Yansheng
Pasquier, Adrien
AuthorAffiliation 14 Institut Hospitalo-Universitaire, Pôle Hépato-digestif, Nouvel Hôpital Civil, Strasbourg, France
10 Department of Biology, Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule, Zurich, Switzerland
7 Department of Nephrology, First Affiliated Hospital, Fujian Medical University, Fuzhou, China
1 Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France
15 ImmunoRhumatologie Moléculaire, INSERM UMR_S1109, LabEx TRANSPLANTEX, Centre de Recherche d'Immunologie et d'Hématologie, Faculté de Médecine, Fédération Hospitalo-Universitaire OMICARE, Fédération de Médecine Translationnelle de Strasbourg, Strasbourg, France
4 Université de Strasbourg, Strasbourg, France
8 State Key Laboratory of Kidney Diseases, National Clinical Research Center of Kidney Diseases, Chinese PLA General Hospital, Beijing, China
13 Faculty of Science, University of Zurich, Zurich, Switzerland
2 Centre National de la Recherche Scientifique, UMR7104, Illkirch, France
5 Laboratoire
AuthorAffiliation_xml – name: 6 State Key Laboratory of Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, Xiamen, Fujian, China
– name: 1 Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France
– name: 3 Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France
– name: 13 Faculty of Science, University of Zurich, Zurich, Switzerland
– name: 7 Department of Nephrology, First Affiliated Hospital, Fujian Medical University, Fuzhou, China
– name: 2 Centre National de la Recherche Scientifique, UMR7104, Illkirch, France
– name: 8 State Key Laboratory of Kidney Diseases, National Clinical Research Center of Kidney Diseases, Chinese PLA General Hospital, Beijing, China
– name: 5 Laboratoire de Biochimie et de Biologie Moléculaire, Nouvel Hôpital Civil, Strasbourg, France
– name: 14 Institut Hospitalo-Universitaire, Pôle Hépato-digestif, Nouvel Hôpital Civil, Strasbourg, France
– name: 12 Unité d'immuno-hématologie pédiatrique, Hôpital Necker-Enfant Malades, Assistance Publique des Hôpitaux de Paris, Paris, France
– name: 9 Institut National de la Santé et de la Recherche Medicale (INSERM), U1110, Institut de Recherche sur les Maladies Virales et Hépatiques, Strasbourg, France
– name: 11 Institut IMAGINE, Sorbonne Paris Cité, Université Paris-Descartes, Paris, France
– name: 15 ImmunoRhumatologie Moléculaire, INSERM UMR_S1109, LabEx TRANSPLANTEX, Centre de Recherche d'Immunologie et d'Hématologie, Faculté de Médecine, Fédération Hospitalo-Universitaire OMICARE, Fédération de Médecine Translationnelle de Strasbourg, Strasbourg, France
– name: 10 Department of Biology, Institute of Molecular Systems Biology, Eidgenössische Technische Hochschule, Zurich, Switzerland
– name: 4 Université de Strasbourg, Strasbourg, France
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  orcidid: 0000-0002-7331-783X
  surname: Zhang
  fullname: Zhang, Zhirong
– sequence: 2
  givenname: Gergö
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  fullname: Meszaros, Gergö
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  surname: He
  fullname: He, Wan-ting
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  orcidid: 0000-0002-6207-545X
  surname: Xu
  fullname: Xu, Yanfang
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  fullname: de Fatima Magliarelli, Helena
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  orcidid: 0000-0002-2626-3912
  surname: Liu
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  surname: Puig Gámez
  fullname: Puig Gámez, Marta
– sequence: 10
  givenname: Alexander
  surname: Goginashvili
  fullname: Goginashvili, Alexander
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  orcidid: 0000-0002-3282-9820
  surname: Pasquier
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  surname: Bielska
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  givenname: Rudolf
  surname: Aebersold
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– sequence: 16
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  givenname: Romeo
  orcidid: 0000-0002-9766-4369
  surname: Ricci
  fullname: Ricci, Romeo
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28716882$$D View this record in MEDLINE/PubMed
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G. Meszaros and W.-t. He contributed equally to this paper.
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Snippet The inflammasomes are multiprotein complexes sensing tissue damage and infectious agents to initiate innate immune responses. Different inflammasomes...
Zhang et al. show that Golgi-mediated protein kinase D (PKD) signaling is required and sufficient for NLRP3 inflammasome activation. PKD at the Golgi...
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StartPage 2671
SubjectTerms Activation
Animals
Assembly
Cytosol
Deactivation
Diglycerides
Diglycerides - metabolism
Endoplasmic reticulum
Endoplasmic Reticulum - physiology
Golgi apparatus
Golgi Apparatus - physiology
Hazards
Humans
Immune response
Inactivation
Inflammasomes
Inflammasomes - physiology
Innate immunity
Kinases
Leukocytes (mononuclear)
Leukocytes, Mononuclear - metabolism
Membranes
Mice
Mice, Inbred C57BL
Mice, Knockout
Mitochondria
Mutation
NLR Family, Pyrin Domain-Containing 3 Protein - physiology
Oligomerization
Peripheral blood mononuclear cells
Phosphorylation
Protein kinase
Protein Kinase C - physiology
Proteins
Signaling
Title Protein kinase D at the Golgi controls NLRP3 inflammasome activation
URI https://www.ncbi.nlm.nih.gov/pubmed/28716882
https://www.proquest.com/docview/1983432654
https://www.proquest.com/docview/1921135534
https://pubmed.ncbi.nlm.nih.gov/PMC5584123
Volume 214
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