Structural Study of the RIPoptosome Core Reveals a Helical Assembly for Kinase Recruitment

Title
Structural Study of the RIPoptosome Core Reveals a Helical Assembly for Kinase Recruitment
Author(s)
박현호장태호chao Zheng[chao Zheng]Jixi Li[Jixi Li]Claire Richards[Claire Richards]Tom Walts[Tom Walts]Hao Wu[Hao Wu]Yu-Shan Hsiao[Yu-Shan Hsiao]
Keywords
CELL-DEATH; PROGRAMMED NECROSIS; CRYSTAL-STRUCTURE; TNF-ALPHA; APOPTOSIS; COMPLEX; NECROPTOSIS; INFLAMMATION; MECHANISM; IMAGES
Issue Date
201408
Publisher
AMER CHEMICAL SOC
Citation
BIOCHEMISTRY, v.53, no.33, pp.5424 - 5431
Abstract
Receptor interaction protein kinase 1 (RIP1) is a molecular cell-fate switch. RIP1, together with Fas-associated protein with death domain (FADD) and caspase-8, forms the RIPoptosome that activates apoptosis. RIP1 also associates with RIP3 to form the necrosome that triggers necroptosis. The RIPoptosome assembles through interactions between the death domains (DDs) of RIP1 and FADD and between death effector domains (DEDs) of FADD and caspase-8. In this study, we analyzed the overall structure of the RIP1 DD/FADD DD complex, the core of the RIPoptosome, by negative-stain electron microscopy and modeling. The results show that RIP1 DD and FADD DD form a stable complex in vitro similar to the previously described Fas DD/FADD DD complex, suggesting that the RIPoptosome and the Fas death-inducing signaling complex share a common assembly mechanism. Both complexes adopt a helical conformation that requires type I, II, and III interactions between the death domains.
URI
http://hdl.handle.net/YU.REPOSITORY/31289http://dx.doi.org/10.1021/bi500585u
ISSN
0006-2960
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이과대학 > 화학생화학부 > Articles
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