| Literature DB >> 11546791 |
B W Jordan1, D Dinev, V LeMellay, J Troppmair, R Gotz, L Wixler, M Sendtner, S Ludwig, U R Rapp.
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.Entities:
Mesh:
Substances:
Year: 2001 PMID: 11546791 DOI: 10.1074/jbc.C100171200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157