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JCS ePress online publication date 19 Oct 2004
doi: 10.1242/jcs.01474

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Research Article

RXR{alpha} acts as a carrier for TR3 nuclear export in a 9-cis retinoic acid-dependent manner in gastric cancer cells


Xiao-Feng Lin, Bi-Xing Zhao, Hang-Zhi Chen, Xiao-Feng Ye, Chao-Yi Yang, Hai-Ying Zhou, Ming-Qing Zhang, Sheng-Cai Lin, and Qiao Wu*
* Author for correspondence (e-mail: xgwu{at}xmu.edu.cn)

Retinoid X receptor (RXR) plays a crucial role in the cross talk between retinoid receptors and other hormone receptors including the orphan receptor TR3, forming different heterodimers that transduce diverse steroid/thyroid hormone signaling. Here we show that RXR{alpha} exhibits nucleocytoplasmic shuttling in MGC80-3 gastric cancer cells and that RXR{alpha} shuttling is energy-dependent through a nuclear pore complex (NPC)-mediated pathway for its import and an intact DNA binding domain-mediated pathway for its export. In the presence of its ligand 9-cis retinoic acid, RXR{alpha} was almost exclusively located in the cytoplasm. More importantly, we also show that RXR{alpha} acts as a carrier to assist translocation of TR3, which plays an important role in apoptosis. Both RXR{alpha} and TR3 colocalized in the nucleus; however, upon stimulation by 9-cis retinoic acid they cotranslocated to the cytoplasm and then localized in the mitochondria. TR3 export depends on RXR{alpha}, as in living cells GFP-TR3 alone did not result in export from the nucleus even in the presence of 9-cis retinoic acid, whereas GFP-TR3 cotransfected with RXR{alpha} was exported out of the nucleus in response to 9-cis retinoic acid. Moreover, specific reduction of RXR{alpha} levels caused by anti-sense RXR{alpha} abolished TR3 nuclear export. In contrast, specific knockdown of TR3 by antisense-TR3 or TR3-siRNA did not affect RXR{alpha} shuttling. These results indicate that RXR{alpha} is responsible for TR3 nucleocytoplasmic translocation, which is facilitated by the RXR{alpha} ligand 9-cis retinoic acid. In addition, mitochondrial TR3, but not RXR{alpha}, was critical for apoptosis, as TR3 mutants that were distributed in the mitochondria induced apoptosis in the presence or absence of 9-cis retinoic acid. These data reveal a novel aspect of RXR{alpha} function, in which it acts as a carrier for nucleocytoplasmic translocation of orphan receptors.
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