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TitleNLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation.
Journal, issue, pagesCell, Vol. 184, Issue 26, Page 6299-6312.e22, Year 2021
Publish dateDec 22, 2021
AuthorsLiudmila Andreeva / Liron David / Shaun Rawson / Chen Shen / Teerithveen Pasricha / Pablo Pelegrin / Hao Wu /
PubMed AbstractThe NACHT-, leucine-rich-repeat- (LRR), and pyrin domain-containing protein 3 (NLRP3) is emerging to be a critical intracellular inflammasome sensor of membrane integrity and a highly important ...The NACHT-, leucine-rich-repeat- (LRR), and pyrin domain-containing protein 3 (NLRP3) is emerging to be a critical intracellular inflammasome sensor of membrane integrity and a highly important clinical target against chronic inflammation. Here, we report that an endogenous, stimulus-responsive form of full-length mouse NLRP3 is a 12- to 16-mer double-ring cage held together by LRR-LRR interactions with the pyrin domains shielded within the assembly to avoid premature activation. Surprisingly, this NLRP3 form is predominantly membrane localized, which is consistent with previously noted localization of NLRP3 at various membrane organelles. Structure-guided mutagenesis reveals that trans-Golgi network dispersion into vesicles, an early event observed for many NLRP3-activating stimuli, requires the double-ring cages of NLRP3. Double-ring-defective NLRP3 mutants abolish inflammasome punctum formation, caspase-1 processing, and cell death. Thus, our data uncover a physiological NLRP3 oligomer on the membrane that is poised to sense diverse signals to induce inflammasome activation.
External linksCell / PubMed:34861190 / PubMed Central
MethodsEM (single particle)
Resolution4.2 - 9.5 Å
Structure data

23302

7lfh

EMDB-23302, PDB-7lfh:
Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer)
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-23303:
Cryo-EM structure of NLRP3 double-ring cage, 6-fold (12-mer)
Method: EM (single particle) / Resolution: 5.8 Å

EMDB-23304:
Cryo-EM structure of NLRP3 double-ring cage, 7-fold (14-mer)
Method: EM (single particle) / Resolution: 7.7 Å

EMDB-23305:
Cryo-EM structure of NLRP3 double-ring cage, 8-fold (16-mer)
Method: EM (single particle) / Resolution: 9.5 Å

Source
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / NLRP3 / NEK7 / nucleotid-binding / ATP-binding / inflammasome / immunity / innate immunity / NACHT / LRR / PYD

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