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Originally published In Press as doi:10.1074/jbc.C100171200 on September 6, 2001

J. Biol. Chem., Vol. 276, Issue 43, 39985-39989, October 26, 2001
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Neurotrophin Receptor-interacting Mage Homologue Is an Inducible Inhibitor of Apoptosis Protein-interacting Protein That Augments Cell Death*

Bruce W. M. Jordan, Dragomir Dinev, Veronique LeMellay, Jakob Troppmair, Rudolf Götz, Ludmilla Wixler, Michael SendtnerDagger , Stephan Ludwig, and Ulf R. Rapp§

From the Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), Universität Würzburg, Versbacher Strasse 5, 97078 Würzburg, Germany and the Dagger  Institut für Neurobiology, University of Würzburg, Josef-Schneider-Strasse 11,97080 Würzburg, Germany

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.

* This work was supported by Mildred Scheel Stiftung Grant Az 10-1446-Ra4.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Inst. für Medizinische Strahlenkunde und Zellforschung, Universität Würzburg, Versbacher Str. 5, 97078 Würzburg, Germany. Tel.: 49-931-201-5041; Fax: 49-931-201-3835; E-mail: rappur@mail.uni-wuerzburg.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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