Mechanism of membrane pore formation by human gasdermin‐D
Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N‐terminal domain (GSDMD Nterm ) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the...
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| Published in | The EMBO journal Vol. 37; no. 14 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
13.07.2018
Springer Nature B.V John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0261-4189 1460-2075 1460-2075 |
| DOI | 10.15252/embj.201798321 |
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| Abstract | Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N‐terminal domain (GSDMD
Nterm
) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMD
Nterm
insertion, oligomerization, and pore formation are poorly understood. Here, we apply high‐resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMD
Nterm
inserts and assembles in membranes. We observe GSDMD
Nterm
inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMD
Nterm
assembles arc‐, slit‐, and ring‐shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase‐1, caspase‐4, or caspase‐5. Using time‐lapse AFM, we monitor how GSDMD
Nterm
assembles into arc‐shaped oligomers that can transform into larger slit‐shaped and finally into stable ring‐shaped oligomers. Our observations translate into a mechanistic model of GSDMD
Nterm
transmembrane pore assembly, which is likely shared within the gasdermin protein family.
Synopsis
Gasdermin‐D, which mediates pyroptosis in human and murine cells, is directly observed inserting into lipid membranes and assembling arc‐, slit‐ and ring‐shaped oligomers. The observations translate into a mechanistic model of gasdermin‐D assembling transmembrane lytic pores.
High‐resolution time‐lapse imaging of gasdermin‐D pore formation.
Gasdermin‐D assembles arc‐, slit‐ and ring‐shaped oligomers.
Arc‐ and slit‐shaped pores transform into stable ring‐shaped pores.
Phosphatidylinositide (PI(4,5)P2) increases gasdermin‐D pore formation.
Cholesterol reduces gasdermin‐D pore formation.
Graphical Abstract
High‐resolution atomic force microscopy shows how a pyroptosis‐mediating gasdermin protein inserts into lipid membranes and assembles arc‐, slit‐ and ring‐shaped oligomers. |
|---|---|
| AbstractList | Gasdermin‐D (
GSDMD
), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases,
GSDMD
inserts its N‐terminal domain (GSDMD
Nterm
) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMD
Nterm
insertion, oligomerization, and pore formation are poorly understood. Here, we apply high‐resolution (≤ 2 nm) atomic force microscopy (
AFM
) to describe how GSDMD
Nterm
inserts and assembles in membranes. We observe GSDMD
Nterm
inserting into a variety of lipid compositions, among which phosphatidylinositide (
PI
(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMD
Nterm
assembles arc‐, slit‐, and ring‐shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether
GSDMD
has been cleaved by caspase‐1, caspase‐4, or caspase‐5. Using time‐lapse
AFM
, we monitor how GSDMD
Nterm
assembles into arc‐shaped oligomers that can transform into larger slit‐shaped and finally into stable ring‐shaped oligomers. Our observations translate into a mechanistic model of GSDMD
Nterm
transmembrane pore assembly, which is likely shared within the gasdermin protein family. Gasdermin-D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N-terminal domain (GSDMD ) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMD insertion, oligomerization, and pore formation are poorly understood. Here, we apply high-resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMD inserts and assembles in membranes. We observe GSDMD inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMD assembles arc-, slit-, and ring-shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase-1, caspase-4, or caspase-5. Using time-lapse AFM, we monitor how GSDMD assembles into arc-shaped oligomers that can transform into larger slit-shaped and finally into stable ring-shaped oligomers. Our observations translate into a mechanistic model of GSDMD transmembrane pore assembly, which is likely shared within the gasdermin protein family. Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N‐terminal domain (GSDMDNterm) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMDNterm insertion, oligomerization, and pore formation are poorly understood. Here, we apply high‐resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMDNterm inserts and assembles in membranes. We observe GSDMDNterm inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMDNterm assembles arc‐, slit‐, and ring‐shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase‐1, caspase‐4, or caspase‐5. Using time‐lapse AFM, we monitor how GSDMDNterm assembles into arc‐shaped oligomers that can transform into larger slit‐shaped and finally into stable ring‐shaped oligomers. Our observations translate into a mechanistic model of GSDMDNterm transmembrane pore assembly, which is likely shared within the gasdermin protein family. Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N‐terminal domain (GSDMD Nterm ) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMD Nterm insertion, oligomerization, and pore formation are poorly understood. Here, we apply high‐resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMD Nterm inserts and assembles in membranes. We observe GSDMD Nterm inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMD Nterm assembles arc‐, slit‐, and ring‐shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase‐1, caspase‐4, or caspase‐5. Using time‐lapse AFM, we monitor how GSDMD Nterm assembles into arc‐shaped oligomers that can transform into larger slit‐shaped and finally into stable ring‐shaped oligomers. Our observations translate into a mechanistic model of GSDMD Nterm transmembrane pore assembly, which is likely shared within the gasdermin protein family. Synopsis Gasdermin‐D, which mediates pyroptosis in human and murine cells, is directly observed inserting into lipid membranes and assembling arc‐, slit‐ and ring‐shaped oligomers. The observations translate into a mechanistic model of gasdermin‐D assembling transmembrane lytic pores. High‐resolution time‐lapse imaging of gasdermin‐D pore formation. Gasdermin‐D assembles arc‐, slit‐ and ring‐shaped oligomers. Arc‐ and slit‐shaped pores transform into stable ring‐shaped pores. Phosphatidylinositide (PI(4,5)P2) increases gasdermin‐D pore formation. Cholesterol reduces gasdermin‐D pore formation. Graphical Abstract High‐resolution atomic force microscopy shows how a pyroptosis‐mediating gasdermin protein inserts into lipid membranes and assembles arc‐, slit‐ and ring‐shaped oligomers. Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N‐terminal domain (GSDMDNterm) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMDNterm insertion, oligomerization, and pore formation are poorly understood. Here, we apply high‐resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMDNterm inserts and assembles in membranes. We observe GSDMDNterm inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMDNterm assembles arc‐, slit‐, and ring‐shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase‐1, caspase‐4, or caspase‐5. Using time‐lapse AFM, we monitor how GSDMDNterm assembles into arc‐shaped oligomers that can transform into larger slit‐shaped and finally into stable ring‐shaped oligomers. Our observations translate into a mechanistic model of GSDMDNterm transmembrane pore assembly, which is likely shared within the gasdermin protein family. Synopsis Gasdermin‐D, which mediates pyroptosis in human and murine cells, is directly observed inserting into lipid membranes and assembling arc‐, slit‐ and ring‐shaped oligomers. The observations translate into a mechanistic model of gasdermin‐D assembling transmembrane lytic pores. High‐resolution time‐lapse imaging of gasdermin‐D pore formation. Gasdermin‐D assembles arc‐, slit‐ and ring‐shaped oligomers. Arc‐ and slit‐shaped pores transform into stable ring‐shaped pores. Phosphatidylinositide (PI(4,5)P2) increases gasdermin‐D pore formation. Cholesterol reduces gasdermin‐D pore formation. High‐resolution atomic force microscopy shows how a pyroptosis‐mediating gasdermin protein inserts into lipid membranes and assembles arc‐, slit‐ and ring‐shaped oligomers. Gasdermin-D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N-terminal domain (GSDMDNterm) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMDNterm insertion, oligomerization, and pore formation are poorly understood. Here, we apply high-resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMDNterm inserts and assembles in membranes. We observe GSDMDNterm inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMDNterm assembles arc-, slit-, and ring-shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase-1, caspase-4, or caspase-5. Using time-lapse AFM, we monitor how GSDMDNterm assembles into arc-shaped oligomers that can transform into larger slit-shaped and finally into stable ring-shaped oligomers. Our observations translate into a mechanistic model of GSDMDNterm transmembrane pore assembly, which is likely shared within the gasdermin protein family.Gasdermin-D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts its N-terminal domain (GSDMDNterm) into cellular membranes and assembles large oligomeric complexes permeabilizing the membrane. So far, the mechanisms of GSDMDNterm insertion, oligomerization, and pore formation are poorly understood. Here, we apply high-resolution (≤ 2 nm) atomic force microscopy (AFM) to describe how GSDMDNterm inserts and assembles in membranes. We observe GSDMDNterm inserting into a variety of lipid compositions, among which phosphatidylinositide (PI(4,5)P2) increases and cholesterol reduces insertion. Once inserted, GSDMDNterm assembles arc-, slit-, and ring-shaped oligomers, each of which being able to form transmembrane pores. This assembly and pore formation process is independent on whether GSDMD has been cleaved by caspase-1, caspase-4, or caspase-5. Using time-lapse AFM, we monitor how GSDMDNterm assembles into arc-shaped oligomers that can transform into larger slit-shaped and finally into stable ring-shaped oligomers. Our observations translate into a mechanistic model of GSDMDNterm transmembrane pore assembly, which is likely shared within the gasdermin protein family. |
| Author | Mulvihill, Estefania Pfreundschuh, Moritz Hiller, Sebastian Mari, Stefania A Sborgi, Lorenzo Müller, Daniel J |
| AuthorAffiliation | 1 Department of Biosystems Science and Engineering Eidgenössische Technische Hochschule (ETH) Zurich Basel Switzerland 2 Biozentrum University of Basel Basel Switzerland |
| AuthorAffiliation_xml | – name: 1 Department of Biosystems Science and Engineering Eidgenössische Technische Hochschule (ETH) Zurich Basel Switzerland – name: 2 Biozentrum University of Basel Basel Switzerland |
| Author_xml | – sequence: 1 givenname: Estefania orcidid: 0000-0002-7074-2371 surname: Mulvihill fullname: Mulvihill, Estefania organization: Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich – sequence: 2 givenname: Lorenzo surname: Sborgi fullname: Sborgi, Lorenzo organization: Biozentrum, University of Basel – sequence: 3 givenname: Stefania A surname: Mari fullname: Mari, Stefania A organization: Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich – sequence: 4 givenname: Moritz surname: Pfreundschuh fullname: Pfreundschuh, Moritz organization: Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich – sequence: 5 givenname: Sebastian orcidid: 0000-0002-6709-4684 surname: Hiller fullname: Hiller, Sebastian organization: Biozentrum, University of Basel – sequence: 6 givenname: Daniel J orcidid: 0000-0003-3075-0665 surname: Müller fullname: Müller, Daniel J email: daniel.mueller@bsse.ethz.ch organization: Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29898893$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | The Author(s) 2018 2018 The Authors. Published under the terms of the CC BY 4.0 license 2018 The Authors. Published under the terms of the CC BY 4.0 license. 2018 EMBO |
| Copyright_xml | – notice: The Author(s) 2018 – notice: 2018 The Authors. Published under the terms of the CC BY 4.0 license – notice: 2018 The Authors. Published under the terms of the CC BY 4.0 license. – notice: 2018 EMBO |
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| DOI | 10.15252/embj.201798321 |
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| Keywords | time‐lapse high‐resolution atomic force microscopy transmission electron microscopy cell death gasdermin‐D pore assembly inflammation |
| Language | English |
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Pneumolysin from Streptococcus pneumoniae publication-title: Nano Lett – volume: 16 start-page: 407 year: 2016 end-page: 420 article-title: Inflammasomes: mechanism of assembly, regulation and signalling publication-title: Nat Rev Immunol – volume: 9 start-page: 113 year: 2001 end-page: 114 article-title: Pro‐inflammatory programmed cell death publication-title: Trends Microbiol – volume: 157 start-page: 1013 year: 2014 end-page: 1022 article-title: Mechanisms and functions of inflammasomes publication-title: Cell – volume: 11 start-page: 1136 year: 2010 end-page: 1142 article-title: Caspase‐1‐induced pyroptosis is an innate immune effector mechanism against intracellular bacteria publication-title: Nat Immunol – volume: 547 start-page: 99 year: 2017 end-page: 103 article-title: Chemotherapy drugs induce pyroptosis through caspase‐3 cleavage of a gasdermin publication-title: Nature – volume: 35 start-page: 1766 year: 2016 end-page: 1778 article-title: GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death publication-title: EMBO J – volume: 12 start-page: 467 year: 2017 end-page: 473 article-title: Real‐time visualization of perforin nanopore assembly publication-title: Nat Nanotechnol – volume: 113 start-page: 7858 year: 2016 end-page: 7863 article-title: GsdmD p30 elicited by caspase‐11 during pyroptosis forms pores in membranes publication-title: Proc Natl Acad Sci USA – volume: 93 start-page: 329 year: 2013 end-page: 342 article-title: Current trends in inflammatory and immunomodulatory mediators in sepsis publication-title: J Leukoc Biol – volume: 64 start-page: 1868 year: 1993 end-page: 1873 article-title: Calibration of atomic‐force microscope tips publication-title: Rev Sci Instrum – volume: 35 start-page: 389 year: 2016 end-page: 401 article-title: Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores publication-title: EMBO J – volume: 23 start-page: 3206 year: 2004 end-page: 3215 article-title: Vertical collapse of a cytolysin prepore moves its transmembrane beta‐hairpins to the membrane publication-title: EMBO J – volume: 526 start-page: 666 year: 2015 end-page: 671 article-title: Caspase‐11 cleaves gasdermin D for non‐canonical inflammasome signalling publication-title: Nature – volume: 6 start-page: 8761 year: 2015 article-title: Human caspase‐4 and caspase‐5 regulate the one‐step non‐canonical inflammasome activation in monocytes publication-title: Nat Commun – volume: 16 start-page: 319 year: 2013 end-page: 326 article-title: Inflammasome‐mediated pyroptotic and apoptotic cell death, and defense against infection publication-title: Curr Opin Microbiol – volume: 7 start-page: 57481 year: 2016 end-page: 57482 article-title: The gasdermin‐D pore: executor of pyroptotic cell death publication-title: Oncotarget – volume: 443 start-page: 651 year: 2006 end-page: 657 article-title: Phosphoinositides in cell regulation and membrane dynamics publication-title: 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| Snippet | Gasdermin‐D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts... Gasdermin-D (GSDMD), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts... Gasdermin‐D ( GSDMD ), a member of the gasdermin protein family, mediates pyroptosis in human and murine cells. Cleaved by inflammatory caspases, GSDMD inserts... |
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| SubjectTerms | Assembling Assembly Atomic force microscopy Caspase Caspases - metabolism Cell death Cell Membrane - metabolism Cholesterol EMBO07 EMBO19 gasdermin‐D pore assembly Humans Inflammation Insertion Inserts Lipid membranes Liposomes - metabolism Membranes Metals Microscopy, Atomic Force Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Oligomerization Oligomers Pore formation Pores Porosity Protein Multimerization Protein Transport Proteins Pyroptosis Recombinant Proteins - genetics Recombinant Proteins - metabolism Time-Lapse Imaging time‐lapse high‐resolution atomic force microscopy transmission electron microscopy |
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| Title | Mechanism of membrane pore formation by human gasdermin‐D |
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