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TitleCryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 43, Page 10845-10852, Year 2018
Publish dateOct 23, 2018
AuthorsYang Li / Tian-Min Fu / Alvin Lu / Kristen Witt / Jianbin Ruan / Chen Shen / Hao Wu /
PubMed AbstractCanonical inflammasomes are cytosolic supramolecular complexes that activate caspase-1 upon sensing extrinsic microbial invasions and intrinsic sterile stress signals. During inflammasome assembly, ...Canonical inflammasomes are cytosolic supramolecular complexes that activate caspase-1 upon sensing extrinsic microbial invasions and intrinsic sterile stress signals. During inflammasome assembly, adaptor proteins ASC and NLRC4 recruit caspase-1 through homotypic caspase recruitment domain (CARD) interactions, leading to caspase-1 dimerization and activation. Activated caspase-1 processes proinflammatory cytokines and Gasdermin D to induce cytokine maturation and pyroptotic cell death. Here, we present cryo-electron microscopy (cryo-EM) structures of NLRC4 CARD and ASC CARD filaments mediated by conserved three types of asymmetric interactions (types I, II, and III). We find that the CARDs of these two adaptor proteins share a similar assembly pattern, which matches that of the caspase-1 CARD filament whose structure we defined previously. These data indicate a unified mechanism for downstream caspase-1 recruitment through CARD-CARD interactions by both adaptors. Using structure modeling, we further show that full-length NLRC4 assembles via two separate symmetries at its CARD and its nucleotide-binding domain (NBD), respectively.
External linksProc Natl Acad Sci U S A / PubMed:30279182 / PubMed Central
MethodsEM (helical sym.)
Resolution3.17 - 3.58 Å
Structure data

EMDB-8902: Cryo-EM Structures of ASC and NLRC4 CARD Filaments Reveal a Unified Mechanism of Nucleation and Activation of Caspase-1
PDB-6n1h: Cryo-EM structure of ASC-CARD filament
Method: EM (helical sym.) / Resolution: 3.17 Å

EMDB-8903: Cryo-EM Structures of ASC and NLRC4 CARD Filaments Reveal a Unified Mechanism of Nucleation and Activation of Caspase-1
PDB-6n1i: Cryo-EM structure of NLRC4-CARD filament
Method: EM (helical sym.) / Resolution: 3.58 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Inflammasome / filament / immunity

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