Transactivation function of RXR has been characterized, and the ability of RXR to Steroid and thyroid hormone receptor superfamily. Pathways, either as a homodimer or as a heterodimer, with other members of the The retinoid X receptor (RXR) participates in a wide array of hormonal signaling Involved in mediating retinoid function (Mahajna, 1997). These findings raise the possibility that RXRĪlpha/beta3, and perhaps hRXR beta3 isoform, function by titrating a limiting adaptor molecule that is Responsible for the altered behavior of the chimera. Suggests that the SLSR insertion in the ligand-binding domain of the RXR alpha/beta3 receptor is
Physically with the retinoic acid receptor (RAR) to form heterodimers as detected by physicalĪssociation assays, and fails to bind DNA containing an RAR-responsive element. Moreover, the RXR alpha/beta3 protein fails to interact Receptors on retinoid-responsive promoters. The RXRĪlpha/beta3 receptor exhibits dominant negative activity against active retinoid X and retinoic acid Co-transfectionĪssays reveal that a chimera RXR alpha/beta3 receptor fails to transactivate the RXR-specificĬRBPII promoter, whereas the identical chimera lacking the SLSR insertion is active. Insertion on the transactivation and DNA-binding functions of the chimeric receptor. The corresponding domain from hRXR beta3, were used to investigate the consequences of the SLSR Chimeric receptors, in which the ligand-binding domain of hRXR alpha was substituted by Transcription polymerase chain reaction (RT-PCR) in all human tumor cell lines and mouse tissuesĮxamined. The isoform is generated by alternate use of a 3' splice acceptor site and is detectable by reverse Mammalian RXR - interactions during transcriptional activationĪn isoform of hRXR beta, termed hRXR beta3, contains an in-frame insertion of four amino acids (SLSR) in the ligand binding domain at codon 419.
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