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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Line
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DNA, Complementary / genetics
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DNA-Binding Proteins / antagonists & inhibitors
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Embryo, Mammalian
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Epithelial Cells / metabolism
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Humans
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Immunoglobulin J Recombination Signal Sequence-Binding Protein / genetics
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Immunoglobulin J Recombination Signal Sequence-Binding Protein / metabolism*
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Intracellular Signaling Peptides and Proteins
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Kidney / cytology*
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LIM Domain Proteins
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Muscle Proteins / genetics
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Muscle Proteins / metabolism*
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Plasmids
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Polycomb Repressive Complex 1
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Receptors, Notch / metabolism
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Signal Transduction
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Transcription, Genetic
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Transfection
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Two-Hybrid System Techniques
Substances
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DNA, Complementary
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DNA-Binding Proteins
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FHL1 protein, human
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Immunoglobulin J Recombination Signal Sequence-Binding Protein
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Intracellular Signaling Peptides and Proteins
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LIM Domain Proteins
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Muscle Proteins
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Receptors, Notch
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Recombinant Proteins
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Polycomb Repressive Complex 1
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RING1 protein, human