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Article
Open AccessNLRP inflammasomes in health and disease
NLRP inflammasomes are a group of cytosolic multiprotein oligomer pattern recognition receptors (PRRs) involved in the recognition of pathogen-associated molecular patterns (PAMPs) and danger-associated molecu...
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Article
Regulating GSDMB pore formation: to ignite or inhibit?
In the recent Nature, Wang et al. and Zhong et al. present the cryo-EM structures of Gasdermin B (GSDMB) pore and strucures of GSDMB in complex with a Shigella effector, IpaH7.8. The structures shed light on the ...
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Article
Open AccessStructural basis for GSDMB pore formation and its targeting by IpaH7.8
Gasdermins (GSDMs) are pore-forming proteins that play critical roles in host defence through pyroptosis1,2. Among GSDMs, GSDMB is unique owing to its distinct lipid-binding profile and a lack of consensus on its...
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Article
Open Access3D Artificial Array Interface Engineering Enabling Dendrite-Free Stable Zn Metal Anode
The design concept of 3D artificial array interface engineering was proposed to achieve eliminated volume stress, preferred orientation growth and dendrite-free Zn metal anode.
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Article
Gasdermin D pore structure reveals preferential release of mature interleukin-1
As organelles of the innate immune system, inflammasomes activate caspase-1 and other inflammatory caspases that cleave gasdermin D (GSDMD). Caspase-1 also cleaves inactive precursors of the interleukin (IL)-1...
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Article
Intracellular immune sensing promotes inflammation via gasdermin D–driven release of a lectin alarmin
Inflammatory caspase sensing of cytosolic lipopolysaccharide (LPS) triggers pyroptosis and the concurrent release of damage-associated molecular patterns (DAMPs). Collectively, DAMPs are key determinants that ...
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Article
Open AccessMechanism of filament formation in UPA-promoted CARD8 and NLRP1 inflammasomes
NLRP1 and CARD8 are related cytosolic sensors that upon activation form supramolecular signalling complexes known as canonical inflammasomes, resulting in caspase−1 activation, cytokine maturation and/or pyrop...
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Article
FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation
Cytosolic sensing of pathogens and damage by myeloid and barrier epithelial cells assembles large complexes called inflammasomes, which activate inflammatory caspases to process cytokines (IL-1β) and gasdermin...
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Article
Publisher Correction: SERPINB1-mediated checkpoint of inflammatory caspase activation
In the version of this article initially published, the label (CASP4-C285A-HA) above the second and fifth lanes in the right blot in Fig. 1e is incorrect; the correct label is CASP4-C258A-HA. Also, the two labels...
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Article
SERPINB1-mediated checkpoint of inflammatory caspase activation
Inflammatory caspases (caspase-1, caspase-4, caspase-5 and caspase-11 (caspase-1/-4/-5/-11)) mediate host defense against microbial infections, processing pro-inflammatory cytokines and triggering pyroptosis. ...
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Structural Insight of Gasdermin Family Driving Pyroptotic Cell Death
Gasdermin is a recently identified family of pore-forming proteins consisting of Gasdermin A (GSDMA), Gasdermin B (GSDMB), Gasdermin C (GSDMC), Gasdermin D (GSDMD), Gasdermin E (GSDME), and DFNB59. Gasdermin D...
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Article
Cryo-EM structure of the gasdermin A3 membrane pore
Gasdermins mediate inflammatory cell death after cleavage by caspases or other, unknown enzymes. The cleaved N-terminal fragments bind to acidic membrane lipids to form pores, but the mechanism of pore formati...
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Article
Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores
Caspase-mediated cleavage of gasdermin D, previously shown to mediate pyroptosis, acts by inducing oligomerization and pore formation in cell membranes.
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Article
Open AccessPlasticity in PYD assembly revealed by cryo-EM structure of the PYD filament of AIM2
Absent in melanoma 2 (AIM2) is an essential cytosolic double-stranded DNA receptor that assembles with the adaptor, apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), and caspa...
