Jordan B W, Dinev D, LeMellay V, Troppmair J, Gotz R, Wixler L, Sendtner M, Ludwig S, Rapp U R
Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), Universität Würzburg, Versbacher Strasse 5, 97078 Würzburg, Germany.
J Biol Chem. 2001 Oct 26;276(43):39985-9. doi: 10.1074/jbc.C100171200. Epub 2001 Sep 6.
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.
凋亡抑制蛋白(IAPs)已被证明可与越来越多的细胞内蛋白和信号通路相互作用,以发挥其抗凋亡作用。在寻找新的与IAP相互作用的蛋白时,我们发现神经营养因子受体相互作用MAGE同源物(NRAGE)能够与禽类IAP同源物ITA结合。这种相互作用需要ITA的RING结构域。NRAGE还能与XIAP共同免疫沉淀。当在32D细胞中过表达时,NRAGE可能通过结合内源性XIAP增强白细胞介素-3撤除诱导的细胞凋亡。此外,NRAGE能够克服Bcl-2的抗凋亡作用。