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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Apoptosis / physiology*
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Binding Sites
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Birds
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DNA-Binding Proteins / metabolism*
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Dimerization
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Gene Expression Regulation
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Inhibitor of Apoptosis Proteins
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Insect Proteins
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Interleukin-3 / deficiency
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Mice
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Neoplasm Proteins*
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Protein Binding
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Proteins / metabolism*
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Proto-Oncogene Proteins c-bcl-2 / metabolism
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Tumor Cells, Cultured
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X-Linked Inhibitor of Apoptosis Protein
Substances
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DNA-Binding Proteins
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Inhibitor of Apoptosis Proteins
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Insect Proteins
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Interleukin-3
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Maged1 protein, mouse
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Neoplasm Proteins
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Proteins
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Proto-Oncogene Proteins c-bcl-2
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X-Linked Inhibitor of Apoptosis Protein