Self-oligomerization of ASC PYD Domain Prevents the Assembly of Inflammasome In Vitro
- Self-oligomerization of ASC PYD Domain Prevents the Assembly of Inflammasome In Vitro
- 박현호; 베드리칸난; 장태호
- CRYSTAL-STRUCTURE; PYRIN DOMAIN; NALP3; CASPASE-1; COMPLEX; CRYOPYRIN/NALP3; ACTIVATION; APOPTOSIS; IMMUNITY; PLATFORM
- Issue Date
- HUMANA PRESS INC
- APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.172, no.8, pp.3902 - 3912
- NALP3 inflammasome, which is an inflammatory caspase-activating complex, is composed of three proteins: NALP3 (an NOD-like receptor), an apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), and caspase-1. NALP3 senses danger signals, while ASC is an adaptor molecule containing two protein interaction modules: pyrin domain (PYD) and caspase recruitment domain (CARD). Caspase-1 is a cysteine protease that uses cysteine as a nucleophile and has a CARD domain for protein interaction. During inflammasome formation, the ASC adaptor acts as a bridge between caspase and NOD-like receptor (NLR) by offering the CARD for CARD-CARD interactions and PYD for PYD-PYD interactions. In the current study, we successfully purified and characterized NALP3 PYD and ASC PYD. The results showed that ASC PYD easily self-oligomerized under physiological conditions, and this self-oligomerization of the ASC PYD prevented complex formation with NALP3 PYD in vitro.
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