An Assay for the Seeding of Homotypic Pyrin Domain Filament Transitions.

ASC Electron microscopy Filament elongation Filament nucleation Inflammasome Innate immunity NLRP3 PYD Pyrin domain

Journal

Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969

Informations de publication

Date de publication:
2022
Historique:
entrez: 27 6 2022
pubmed: 28 6 2022
medline: 30 6 2022
Statut: ppublish

Résumé

Pattern recognition receptors of innate immune cells allow the recognition of invariant microbial structures. The nucleotide-binding oligomerization domain-like receptors (NLRs) comprise 22 members, divided into 3 subfamilies. Homotypic pyrin domain (PYD) interactions were shown to mediate the interaction of inflammasome forming NLRPs with the adaptor protein ASC, bridging the interaction to caspase-1 and resulting in caspase-1-induced cytokine maturation and pyroptotic cell death. Here we describe a NLRP3

Identifiants

pubmed: 35759199
doi: 10.1007/978-1-0716-2449-4_13
doi:

Substances chimiques

Cytoskeletal Proteins 0
NLR Family, Pyrin Domain-Containing 3 Protein 0
Caspase 1 EC 3.4.22.36

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

197-207

Informations de copyright

© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Références

Martinon F, Burns K, Tschopp J (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 10:417–426. https://doi.org/10.1016/s1097-2765(02)00599-3
doi: 10.1016/s1097-2765(02)00599-3 pubmed: 12191486
Kufer TA, Sansonetti PJ (2011) NLR functions beyond pathogen recognition. Nat Immunol 12:121–128. https://doi.org/10.1038/ni.1985
doi: 10.1038/ni.1985 pubmed: 21245903
Franchi L, Muñoz-Planillo R, Núñez G (2012) Sensing and reacting to microbes via the inflammasomes. Nat Immunol 13:325–332. https://doi.org/10.1038/ni.2231
doi: 10.1038/ni.2231 pubmed: 22430785 pmcid: 3449002
Latz E, Xiao TS, Stutz A (2013) Activation and regulation of the inflammasomes. Nat Rev Immunol 13:397–411. https://doi.org/10.1038/nri3452
doi: 10.1038/nri3452 pubmed: 23702978
Stutz A, Kolbe C-C, Stahl R et al (2017) NLRP3 inflammasome assembly is regulated by phosphorylation of the pyrin domain. J Exp Med 214:1725–1736. https://doi.org/10.1084/jem.20160933
doi: 10.1084/jem.20160933 pubmed: 28465465 pmcid: 5460996
Marleaux M, Anand K, Latz E, Geyer M (2020) Crystal structure of the human NLRP9 pyrin domain suggests a distinct mode of inflammasome assembly. FEBS Lett 594:2383–2395. https://doi.org/10.1002/1873-3468.13865
doi: 10.1002/1873-3468.13865 pubmed: 32542665
Fernandes-Alnemri T, Wu J, Yu J-W et al (2007) The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation. Cell Death Differ 14:1590–1604. https://doi.org/10.1038/sj.cdd.4402194
doi: 10.1038/sj.cdd.4402194 pubmed: 17599095
Hochheiser IV, Behrmann H, Hagelueken G et al (2022) Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation. Sci Adv 8:eabn7583. https://doi.org/10.1126/sciadv.abn7583
Tropea JE, Cherry S, Waugh DS (2009) Expression and purification of soluble His6-tagged TEV protease. In: Doyle SA (ed) High throughput protein expression and purification: methods and protocols. Humana Press, Totowa, pp 297–307
doi: 10.1007/978-1-59745-196-3_19
Venegas C, Kumar S, Franklin BS et al (2017) Microglia-derived ASC specks cross-seed amyloid-β in Alzheimer’s disease. Nature 552:355–361. https://doi.org/10.1038/nature25158
doi: 10.1038/nature25158 pubmed: 29293211

Auteurs

Inga V Hochheiser (IV)

Institute of Structural Biology, University Hospital Bonn, University of Bonn, Bonn, Germany.

Matthias Geyer (M)

Institute of Structural Biology, University Hospital Bonn, University of Bonn, Bonn, Germany. matthias.geyer@uni-bonn.de.

Articles similaires

Conservation of the cooling agent binding pocket within the TRPM subfamily.

Kate Huffer, Matthew C S Denley, Elisabeth V Oskoui et al.
1.00
TRPM Cation Channels Animals Binding Sites Mice Pyrimidinones
Fucosyltransferases Drug Repositioning Molecular Docking Simulation Molecular Dynamics Simulation Humans
Receptor, Cannabinoid, CB1 Ligands Molecular Dynamics Simulation Protein Binding Thermodynamics
Sirtuin 1 Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha Animals Resveratrol Rats

Classifications MeSH