Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation.
作者： Benjamin Faustin , Lydia Lartigue , Jean-Marie Bruey , Frederic Luciano , Eduard Sergienko
DOI: 10.1016/J.MOLCEL.2007.01.032
关键词: Signal transducing adaptor protein 、 Biology 、 NLR Proteins 、 Protein structure 、 Apoptosome 、 Caspase 1 、 Cell biology 、 Biochemistry 、 AIM2 、 Inflammasome 、 Nod Signaling Adaptor Proteins
摘要: Interleukin (IL)-1beta maturation is accomplished by caspase-1-mediated proteolysis, an essential element of innate immunity. NLRs constitute a recently recognized family caspase-1-activating proteins, which contain nucleotide-binding oligomerization domain and leucine-rich repeat (LRR) domains assemble into multiprotein complexes to create platforms called "inflammasomes." Using purified recombinant we have reconstituted the NALP1 inflammasome characterized requirements for assembly caspase-1 activation. Oligomerization activation occur via two-step mechanism, requiring microbial product, muramyl-dipeptide, component peptidoglycan, followed ribonucleoside triphosphates. Caspase-1 does not require but enhanced adaptor protein ASC. The findings provide biochemical basis understanding how function are regulated, shed light on as direct sensor bacterial components in host defense against pathogens.
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