![]() However, RaRF overexpression promoted nucleolar translocation of E1A from the nucleoplasm. Further fluorescence microscopy indicated that E1A and RaRF were located in the nucleoplasm and nucleolus, respectively. An in vitro glutathione-S-transferase (GST) pull-down assay was used to confirm the direct interaction between E1A and RaRF. The first coiled-coil domain of RaRF was sufficient for this interaction. Based on immunoprecipitation (IP) assays, E1A interacts with RaRF through the conserved region 2 (CR2), which is also responsible for pRb binding. Here, we report how adenovirus E1A stimulates RAR activity by associating with RaRF. Recently, we identified a novel corepressor of RAR called the retinoic acid resistance factor ( RaRF) (manuscript submitted). ![]() Transcriptional activity of the retinoic acid receptor ( RAR) is regulated by diverse binding partners, including classical corepressors and coactivators, in response to its ligand retinoic acid ( RA). De-repression of RaRF-mediated RAR repression by adenovirus E1A in the nucleolus.
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