Abstract
The inhibitor of apoptosis proteins (IAPs) have been shown to interact with a growing number of intracellular proteins and pathways to fulfil their anti-apoptotic role. In the search for novel IAP-interacting proteins we identified the neurotrophin receptor-interacting MAGE homologue (NRAGE) as being able to bind to the avian IAP homologue ITA. This interaction requires the RING domain of ITA. NRAGE additionally coimmunoprecipitates with XIAP. When overexpressed in 32D cells NRAGE augments interleukin-3 withdrawal induced apoptosis, possibly through binding endogenous XIAP. Moreover, NRAGE is able to overcome the anti-apoptotic effect of Bcl-2.
Highlights
The inhibitor of apoptosis proteins (IAPs)1 are encoded by a recently identified family of highly conserved genes, playing a crucial role in the regulation of apoptosis by interfering with the process of caspase activation [1]
In the search for novel IAP-interacting proteins we identified the neurotrophin receptor-interacting melanoma associated antigen (MAGE) homologue (NRAGE) as being able to bind to the avian IAP homologue inhibitor of T cell apoptosis (ITA)
CIAP1 and cIAP2 were originally identified as part of the TNFR2-TRAF signaling complex, with the baculovirus IAP repeat (BIR) domains being responsible for the interaction with TRAFs 1 and 2 [3]
Summary
The inhibitor of apoptosis proteins (IAPs)1 are encoded by a recently identified family of highly conserved genes, playing a crucial role in the regulation of apoptosis by interfering with the process of caspase activation [1]. We show that NRAGE coprecipitates with ITA and XIAP, via the RING zinc finger domain of the IAPs. NRAGE can augment cell death upon growth factor withdrawal in the IL-3-dependent promyeloid leukemic 32D cell line, even in the presence of Bcl-2.
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