Hong-yan Qin1, Hua Han. 1. Department of Medical Genetics and Developmental Biology, Fourth Military Medical University, Xi'an 710032, China.
Abstract
AIM: To investigate the physical interaction between KyoT2 and KyoT2-binding protein 1 (KBP1) and the effect of KBP1 on RBP-J-mediated transcriptional activity. METHODS: GST-pull down, co-immunoprecipitation, mammalian cell two hybrid assay and reporter gene assay were used to examine the physical and functional interactions between KyoT2 and KBP1. RESULTS: KBP1 and KyoT2 could interact with each other both in-vitro and in-vivo, and overexpression of KBP1 could antagonize the suppressive effect of RING1 on RBP-J. CONCLUSION: KBP1 may indirectly modulate Notch signaling pathway by competing with RING1 for binding sites on KyoT2.
AIM: To investigate the physical interaction between KyoT2 and KyoT2-binding protein 1 (KBP1) and the effect of KBP1 on RBP-J-mediated transcriptional activity. METHODS: GST-pull down, co-immunoprecipitation, mammalian cell two hybrid assay and reporter gene assay were used to examine the physical and functional interactions between KyoT2 and KBP1. RESULTS:KBP1 and KyoT2 could interact with each other both in-vitro and in-vivo, and overexpression of KBP1 could antagonize the suppressive effect of RING1 on RBP-J. CONCLUSION:KBP1 may indirectly modulate Notch signaling pathway by competing with RING1 for binding sites on KyoT2.