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Details on Person During inflammasome assembly, NLRP3 oligomers recruit the ap...

Class:IdSummation:9712443
_displayNameDuring inflammasome assembly, NLRP3 oligomers recruit the ap...
_timestamp2021-06-29 20:55:58
created[InstanceEdit:9712445] Shamovsky, Veronica, 2021-01-21
literatureReference[LiteratureReference:9712366] Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
[LiteratureReference:9712343] Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
[LiteratureReference:9713596] Inflammasomes: mechanism of assembly, regulation and signalling
[LiteratureReference:9713591] Structural and dynamics aspects of ASC speck assembly
[LiteratureReference:9713600] Assembly and regulation of ASC specks
[LiteratureReference:9735687] Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1
[LiteratureReference:9735637] ASC filament formation serves as a signal amplification mechanism for inflammasomes
[LiteratureReference:9735652] Structure and interdomain dynamics of apoptosis-associated speck-like protein containing a CARD (ASC)
[LiteratureReference:9735655] ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells
[LiteratureReference:9735666] The pyroptosome: a supramolecular assembly of ASC dimers mediating inflammatory cell death via caspase-1 activation
[LiteratureReference:9735667] Inflammasome and Caspase-1 Activity Characterization and Evaluation: An Imaging Flow Cytometer-Based Detection and Assessment of Inflammasome Specks and Caspase-1 Activation
[LiteratureReference:9735658] Detection of ASC Speck Formation by Flow Cytometry and Chemical Cross-linking
[LiteratureReference:9735640] Evaluation of Canonical Inflammasome Activation in Human Monocytes by Imaging Flow Cytometry
[LiteratureReference:9735649] Structure, Activation and Regulation of NLRP3 and AIM2 Inflammasomes
[LiteratureReference:9735664] Kinetic properties of ASC protein aggregation in epithelial cells
[LiteratureReference:9735654] Comprehensive review of ASC structure and function in immune homeostasis and disease
modified[InstanceEdit:9713598] Shamovsky, Veronica, 2021-01-27
[InstanceEdit:9735688] Shamovsky, Veronica, 2021-06-29
textDuring inflammasome assembly, NLRP3 oligomers recruit the apoptosis-associated speck-like protein containing a CARD (ASC), which in turn oligomerizes to form a perinuclear structure called the ASC speck (Masumoto J et al. 1999; de Alba E 2009; Sahillioglu AC et al. 2014; Dick MS et al. 2016; Hoss F et al. 2018; Nagar A et al. 2019; Lage SL et al. 2019). Kinetic studies showed that ASC rapidly aggregates (within 3 min) to form a speck following inflammasome stimulation (Fernandes-Alnemri T et al. 2007; Cheng J et al. 2010). The ASC protein, encoded by the PYCARD gene, contains a pyrin domain (PYD) and a caspase activation and recruitment domain (CARD), which are connected by a 23 aa linker region (de Alba E 2009; Sahillioglu AC et al. 2014; Hoss F et al. 2016). Structural, dynamics and mutagenesis studies revealed that formation of the PYCARD (ASC) speck is based on specific homophilic interactions of its domains (PYD:PYD, CARD:CARD) (Lu A et al. 2014; Sahillioglu AC et al. 2014; Dick MS et al. 2016; reviewed in Agrawal I & Jha S 2020; Sharma M & de Alba E 2021). The PYCARD (ASC) speck assembly involves self-oligomerization via PYD:PYD interactions to form long filaments (Lu A et al. 2014; Cai X et al. 2014; Dick MS et al. 2016). Targeted mutagenesis and structural analysis revealed that PYD self-interaction is charge-based and is stabilized by several interfaces (Lu A et al. 2014; Sahillioglu AC et al. 2014; reviewed in Hoss F et al. 2016). The CARD:CARD interaction is thought to link individual PYCARD filaments towards forming the dense macromolecular speck (Dick MS et al. 2016). The size of the ASC speck can reach around 1 μm (Lu A et al. 2014; Dick MS et al. 2016). Activated PYCARD (ASC) recruits pro-caspase-1 (CASP1) through homotypic CARD interactions, leading to CASP1 activation through proximity-induced autoproteolysis (Fernandes-Alnemri T et al. 2007; Lu A et al. 2014; Li Y et al. 2018; reviewed in Broz P & Dixit VM 2016).
(summation)[Polymerisation:9712442] PYCARD (ASC) forms oligomers [Homo sapiens]
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