Pannexin‐1 limits the production of proinflammatory cytokines during necroptosis
The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the...
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| Published in | EMBO reports Vol. 20; no. 10; pp. e47840 - n/a |
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| Main Authors | , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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London
Nature Publishing Group UK
04.10.2019
Springer Nature B.V EMBO Press John Wiley and Sons Inc |
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| Abstract | The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin‐1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane “leakiness” requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin‐8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis.
Synopsis
The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines.
Pannexin‐1 is activated concomitantly to phosphatidylserine exposure during early steps of necroptosis.
Activation of Pannexin‐1 by MLKL oligomers requires intracellular vesicles trafficking.
Pannexin‐1 is dispensable for necroptotic cell death.
Pannexin‐1 restrains the production of proinflammatory cytokines associated with necroptosis.
Graphical Abstract
The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines. |
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| AbstractList | The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin‐1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane “leakiness” requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin‐8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis.
Synopsis
The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines.
Pannexin‐1 is activated concomitantly to phosphatidylserine exposure during early steps of necroptosis.
Activation of Pannexin‐1 by MLKL oligomers requires intracellular vesicles trafficking.
Pannexin‐1 is dispensable for necroptotic cell death.
Pannexin‐1 restrains the production of proinflammatory cytokines associated with necroptosis.
The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines. The activation of mixed lineage kinase-like (MLKL) by receptor-interacting protein kinase-3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis-deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin-1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane "leakiness" requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin-8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis.The activation of mixed lineage kinase-like (MLKL) by receptor-interacting protein kinase-3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis-deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin-1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane "leakiness" requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin-8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis. The activation of mixed lineage kinase‐like ( MLKL ) by receptor‐interacting protein kinase‐3 ( RIPK 3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin‐1 ( PANX 1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane “leakiness” requires the small GTP ase RAB 27A and RAB 27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX 1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin‐8, indicating that PANX 1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL , RAB 27, and PANX 1 and propose ways to interfere with inflammation associated with necroptosis. The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin‐1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane “leakiness” requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin‐8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis. The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apoptosis‐deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proinflammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin‐1 (PANX1) channels, concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane “leakiness” requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellular vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin‐8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis. Synopsis The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines. Pannexin‐1 is activated concomitantly to phosphatidylserine exposure during early steps of necroptosis. Activation of Pannexin‐1 by MLKL oligomers requires intracellular vesicles trafficking. Pannexin‐1 is dispensable for necroptotic cell death. Pannexin‐1 restrains the production of proinflammatory cytokines associated with necroptosis. Graphical Abstract The activation of MLKL by RIPK3 controls the execution of necroptosis. During the early stages of necroptotic cell death, MLKL oligomers promote the activation of Pannexin‐1 channels, which constricts the production of proinflammatory cytokines. The activation of mixed lineage kinase-like (MLKL) by receptor-interacting protein kinase-3 (RIPK3) controls the execution of necroptosis, a regulated form of necrosis that occurs in apopto-sis-deficient conditions. Active oligomerized MLKL triggers the exposure of phosphatidylserine residues on the cell surface and disrupts the plasma membrane integrity by forming lytic pores. MLKL also governs endosomal trafficking and biogenesis of small extracellular vesicles as well as the production of proin-flammatory cytokines during the early steps of necroptosis; however, the molecular basis continues to be elucidated. Here, we find that MLKL oligomers activate Pannexin-1 (PANX1) channels , concomitantly to the loss of phosphatidylserine asymmetry. This plasma membrane "leakiness" requires the small GTPase RAB27A and RAB27B isoforms, which regulate intracellu-lar vesicle trafficking, docking, and fusion with the plasma membrane. Although cells in which PANX1 is silenced or inhibited normally undergo necroptotic death, they display enhanced production of cytokines such as interleukin-8, indicating that PANX1 may tamper with inflammation. These data identify a novel signaling nexus between MLKL, RAB27, and PANX1 and propose ways to interfere with inflammation associated with necroptosis. |
| Author | Hulin, Philippe Douanne, Tiphaine Thys, An Papin, Antonin Feyeux, Magalie Gavard, Julie André‐Grégoire, Gwennan Trillet, Kilian Bidère, Nicolas Chiron, David |
| AuthorAffiliation | 4 Institut de Cancérologie de l'Ouest Site René Gauducheau Saint‐Herblain France 1 CRCINA, INSERM, CNRS Université de Nantes Université d'Angers Nantes France 3 L'Héma‐NexT, i‐Site NexT Nantes France 2 GDR3697 Micronit CNRS Nantes France 5 MicroPICell Imaging Core Facility SFR Santé F. Bonamy UMS016 INSERM, CNRS Université de Nantes Nantes France |
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| PublicationDate_xml | – month: 10 year: 2019 text: 04 October 2019 day: 04 |
| PublicationDecade | 2010 |
| PublicationPlace | London |
| PublicationPlace_xml | – name: London – name: England – name: New York – name: Hoboken |
| PublicationTitle | EMBO reports |
| PublicationTitleAbbrev | EMBO Rep |
| PublicationTitleAlternate | EMBO Rep |
| PublicationYear | 2019 |
| Publisher | Nature Publishing Group UK Springer Nature B.V EMBO Press John Wiley and Sons Inc |
| Publisher_xml | – name: Nature Publishing Group UK – name: Springer Nature B.V – name: EMBO Press – name: John Wiley and Sons Inc |
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| Snippet | The activation of mixed lineage kinase‐like (MLKL) by receptor‐interacting protein kinase‐3 (RIPK3) controls the execution of necroptosis, a regulated form of... The activation of mixed lineage kinase-like (MLKL) by receptor-interacting protein kinase-3 (RIPK3) controls the execution of necroptosis, a regulated form of... The activation of mixed lineage kinase‐like ( MLKL ) by receptor‐interacting protein kinase‐3 ( RIPK 3) controls the execution of necroptosis, a regulated form... |
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| StartPage | e47840 |
| SubjectTerms | Activation Apoptosis Cancer Cell death Cell Membrane - metabolism Cell Membrane Permeability Cell surface Cell Survival Channel pores Channels Connexins - metabolism Cytokines Cytokines - metabolism EMBO07 EMBO19 EMBO20 Gene Silencing Guanosine triphosphatases HT29 Cells Humans Inflammation Inflammation Mediators - metabolism Interleukins Intracellular Isoforms Kinases Life Sciences MAP kinase Membrane fusion MLKL Mortality Necroptosis Necrosis Nerve Tissue Proteins - metabolism Oligomerization Oligomers Pannexin‐1 Phosphatidylserine Protein kinase Protein Kinases - metabolism Protein Multimerization Transport Vesicles - metabolism Vesicles |
| Title | Pannexin‐1 limits the production of proinflammatory cytokines during necroptosis |
| URI | https://link.springer.com/article/10.15252/embr.201947840 https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembr.201947840 https://www.ncbi.nlm.nih.gov/pubmed/31410978 https://www.proquest.com/docview/2300539671 https://www.proquest.com/docview/2273232107 https://inserm.hal.science/inserm-02281304 https://pubmed.ncbi.nlm.nih.gov/PMC6776911 |
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