ZFP36 stabilizes RIP1 via degradation of XIAP and cIAP2 thereby promoting ripoptosome assembly
نویسندگان
چکیده
منابع مشابه
cIAP2 supports viability of mice lacking cIAP1 and XIAP.
I nitially classified as potent suppressors of programed cell death, members of the inhibitor of apoptosis (IAP) family have emerged as complex signaling proteins whose functions are not limited to apoptosis regulation, but extend to several signaling pathways involved in the regulation of immunity, inflammation, and cell migration (Gyrd-Hansen & Meier, 2010). Of the eight mammalian IAPs, X-lin...
متن کاملStructural Study of the RIPoptosome Core Reveals a Helical Assembly for Kinase Recruitment
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 ...
متن کاملXIAP inhibits autophagy via XIAP-Mdm2-p53 signalling.
The primary role of autophagy is adaption to starvation. However, increasing evidence suggests that autophagy inhibition also plays an important role in tumorigenesis. Upregulation of X-linked inhibitor of apoptosis (XIAP) has been associated to a variety of human cancers, yet the underlying mechanisms remain obscure. Here, we report that XIAP suppresses autophagy by exerting a previously unide...
متن کاملXIAP inhibits autophagy via XIAP-Mdm2-p53 signaling
All reviewers appreciate the concept of your study and acknowledge a potential interest to a wide audience. Nevertheless, they do raise a number of important concerns, and emphasize that a substantial revision of the manuscript will be required. I would like to highlight that following the suggestions of reviewer #1, the physiological relevance of your observations needs to be addressed. Furthe...
متن کاملcIAPs Block Ripoptosome Formation, a RIP1/Caspase-8 Containing Intracellular Cell Death Complex Differentially Regulated by cFLIP Isoforms
The intracellular regulation of cell death pathways by cIAPs has been enigmatic. Here we show that loss of cIAPs promotes the spontaneous formation of an intracellular platform that activates either apoptosis or necroptosis. This 2 MDa intracellular complex that we designate "Ripoptosome" is necessary but not sufficient for cell death. It contains RIP1, FADD, caspase-8, caspase-10, and caspase ...
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ژورنال
عنوان ژورنال: BMC Cancer
سال: 2015
ISSN: 1471-2407
DOI: 10.1186/s12885-015-1388-5