An updated view on the structure and function of PYRIN domains

被引：31

作者：

Chu, Lan Hoang ^{[1
]}

Gangopadhyay, Anu ^{[1
]}

Dorfleutner, Andrea ^{[1
]}

Stehlik, Christian ^{[1
]}

机构：

[1] Northwestern Univ, Dept Med, Feinberg Sch Med, Div Rheumatol, Chicago, IL 60611 USA

来源：

APOPTOSIS | 2015年 / 20卷 / 02期

基金：

美国国家卫生研究院;

关键词：

PYRIN domain (PYD); Inflammasome; Inflammation; Nod-like receptor (NLR); AIM2-like receptor (ALR); PYRIN domain-only protein (POP); NF-KAPPA-B; NONCANONICAL INFLAMMASOME ACTIVATION; NECROSIS-FACTOR-ALPHA; SPECK-LIKE PROTEIN; CRYSTAL-STRUCTURE; ONLY PROTEIN; 3-DIMENSIONAL STRUCTURE; RIG-I; NEGATIVE REGULATOR; COLON INFLAMMATION;

D O I：

10.1007/s10495-014-1065-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The PYRIN domain (PYD) is a protein-protein interaction domain, which belongs to the death domain fold (DDF) superfamily. It is best known for its signaling function in innate immune responses and particularly in the assembly of inflammasomes, which are large protein complexes that allow the induced proximity-mediated activation of caspase-1 and subsequently the release of pro-inflammatory cytokines. The molecular mechanism of inflammasome assembly was only recently elucidated and specifically requires PYD oligomerization. Here we discuss the recent advances in our understanding of PYD signaling and its regulation by PYD-only proteins.

引用

页码：157 / 173

页数：17

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