An updated view on the structure and function of PYRIN domains

Lan Hoang Chu; Anu Gangopadhyay; Andrea Dorfleutner; Christian Stehlik

doi:10.1007/s10495-014-1065-1

An updated view on the structure and function of PYRIN domains

Lan Hoang Chu, Anu Gangopadhyay, Andrea Dorfleutner^*, Christian Stehlik

^*Corresponding author for this work

Medicine, Rheumatology Division

Research output: Contribution to journal › Article › peer-review

32 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	157-173
Number of pages	17
Journal	Apoptosis
Volume	20
Issue number	2
DOIs	https://doi.org/10.1007/s10495-014-1065-1
State	Published - Feb 2015

Keywords

AIM2-like receptor (ALR)
Inflammasome
Inflammation
Nod-like receptor (NLR)
PYRIN domain (PYD)
PYRIN domain-only protein (POP)

ASJC Scopus subject areas

Biochemistry, medical
Cancer Research
Clinical Biochemistry
Cell Biology
Pharmacology
Pharmaceutical Science

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/s10495-014-1065-1

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title = "An updated view on the structure and function of PYRIN domains",

abstract = "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.",

keywords = "AIM2-like receptor (ALR), Inflammasome, Inflammation, Nod-like receptor (NLR), PYRIN domain (PYD), PYRIN domain-only protein (POP)",

author = "Chu, {Lan Hoang} and Anu Gangopadhyay and Andrea Dorfleutner and Christian Stehlik",

note = "Funding Information: This work was supported by the National Institutes of Health (GM071723, AI099009 and AR064349 to C.S., and AR057532 to A.D.) and the American Heart Association (12GRNT12080035 to C.S). Publisher Copyright: {\textcopyright} 2014 Springer Science+Business Media New York.",

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AU - Gangopadhyay, Anu

AU - Dorfleutner, Andrea

AU - Stehlik, Christian

N1 - Funding Information: This work was supported by the National Institutes of Health (GM071723, AI099009 and AR064349 to C.S., and AR057532 to A.D.) and the American Heart Association (12GRNT12080035 to C.S). Publisher Copyright: © 2014 Springer Science+Business Media New York.

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KW - AIM2-like receptor (ALR)

KW - Inflammasome

KW - Inflammation

KW - Nod-like receptor (NLR)

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KW - PYRIN domain-only protein (POP)

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An updated view on the structure and function of PYRIN domains

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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