Structural basis for termination of AIM2-mediated signaling by p202
Dear Editor,
Sighting and binding of double-stranded DNA (dsDNA) by a sensor in the cytoplasm trigger the activation of the immune-surveillance pathways [1].The crystal structure of absent in melanoma 2 (AIM2) bound with DNA conclusively defines the role of AIM2 as a sensor in the innate immune system [2].AIM2 belongs to the PYHIN family of proteins and contains a pyrin domain (PYD) followed by a hematopoietic interferon-inducible nuclear protein (HIN) domain (Figure 1A).AIM2 binds DNA via the HIN domain and recruits the adaptor protein apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) via the PYD.ASC in turn recruits caspase-1 via CARD-CARD interaction,resulting in the formation of inflammasomes comprised of AIM2,ASC and caspase-1.The molecular crowding of the AIM2 inflammasome ensures the proteolysis and transactivation of caspase-1.Activated caspase-1 cleaves pro-IL-1 β and pro-IL-18 into their mature proinflammatory forms [3,4].
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grants from the Ministry of Health of China2013ZX10004-602;the Ministry of Science and Technology of China2013CB911103,2009CB918803,2011CB911103;the National Natural Science Foundation of China31270795,31200559,31070660,31021062
2013-07-29（万方平台首次上网日期，不代表论文的发表时间）
共4页
855-858
