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AIM2 inflammasome activation and regulation

Title: AIM2 inflammasome activation and regulation: A structural perspective.
Name(s): Wang, Bing, author
Yin, Qian, author
Type of Resource: text
Genre: Journal Article
Date Issued: 2017-12-01
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: Absent in melanoma 2 (AIM2) inflammasome is a multi-protein platform that recognizes aberrant cytoplasmic dsDNA and induces cytokine maturation, release and pyroptosis. It is composed of AIM2, apoptosis-associated speck-like protein containing a CARD (ASC), and caspase-1. Recent X-ray crystallographic and high resolution cryo-electron microscopic (cryo-EM) studies have revealed a series of structures in AIM2 inflammasome activation and regulation. One prominent feature common in multiple steps is the assembly of high-order structures, especially helical filaments nucleated by upstream molecules, rather than stoichiometric complexes. In this review, we track the AIM2 inflammasome activation process step by step, using high-resolution structures to illustrate the overall architecture of AIM2 inflammasome and its assembly and regulatory mechanisms.
Identifier: FSU_pmch_28813641 (IID), 10.1016/j.jsb.2017.08.001 (DOI), PMC5733693 (PMCID), 28813641 (RID), 28813641 (EID), S1047-8477(17)30132-6 (PII)
Keywords: AIM2, ASC, CARD, Caspase-1, Helical filament, High-order assembly, INCA, Inflammasome, P202, PYD, Polymerization
Grant Number: R00 AI108793
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at
Subject(s): Caspase 1/chemistry
Caspase 1/metabolism
Cryoelectron Microscopy
DNA-Binding Proteins/chemistry
DNA-Binding Proteins/metabolism
Intracellular Signaling Peptides and Proteins/metabolism
Nuclear Proteins/metabolism
Persistent Link to This Record:
Host Institution: FSU
Is Part Of: Journal of structural biology.
Issue: iss. 3, vol. 200

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Wang, B., & Yin, Q. (2017). AIM2 inflammasome activation and regulation: A structural perspective. Journal Of Structural Biology. Retrieved from