Abstract
Abstract Telomeres are repetitive sequences at the ends of chromosomes protected by DNA binding proteins of shelterin complex that form capping structures. One of these proteins, TRF1, plays a role in the regulation of telomere length through its interaction with other proteins in the shelterin complex. High levels of TRF1 expression have been shown to accelerate telomere shortening, whereas dominant-negative inhibition of TRF1 leads to telomere elongation. Recently, the newly identified Zinc finger and SCAN domain containing4 gene (ZSCAN4) plays a key role in genomic stability by regulating telomere elongation and was shown to co-localize with TRF1 foci in mouse embryonic stem cell. Here, we show that ZSCAN4 is a TRF1 association protein in breast cancer cells. We hypothesized that ZSCAN4 would affect levels of TRF1expression and correspondingly control the function of TRF1 through negative regulation and dominant-negative inhibition. Using Co-immunoprecipitation and TNT Pull-down assay, we demonstrate that ZSCAN4 binds with TRF1 in vitro. Localization and visualization of interacting protein-protein interactions in living cells are crucial to elucidate between TRF1 and ZSCAN4. Using a bimolecular fluorescence complementation (BiFC) assay, we show the directly visualize TRF1 and ZSCAN4 interactions in living cells. Using telomere length assays, we demonstrate that ZSCAN4 is an association protein of TRF1 to regulate telomere and affect in the telomere elongation of cancer. The ZSCAN4 mediated cooperative binding of TRF1 to telomeric DNA has important implications for understanding the mechanism of telomere extension. Citation Format: kyungwoo lee. The interaction of ZSCAN4 with TRF1: effects on regulation of telomere elongation in cancer cells. [abstract]. In: Proceedings of the 104th Annual Meeting of the American Association for Cancer Research; 2013 Apr 6-10; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2013;73(8 Suppl):Abstract nr 579. doi:10.1158/1538-7445.AM2013-579
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