Abstract
Notch signaling plays a pivotal role in numerous cell fate determination events during development, and therefore its regulation has been studied intensively. MSX2-interacting nuclear target protein (MINT) modifies the Notch signaling by interacting with and inhibiting the downstream transcription factor RBP-J/CBF-1 of Notch. In this study, by a yeast two hybrid screening, we found that the C terminal fragment of MINT interacted with each other. We confirmed the interaction between two MINT C terminal fragments both in vitro and in vivo. We further demonstrated that the overexpression of the C terminal fragment of MINT cancelled its inhibitory effect on the transactivation of an RBP-J-dependent promoter by Notch. These results suggest that MINT may form a dimer or multimer in cells through its C terminus, and that the C terminal fragment of MINT may work as its dominant-negative version.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Animals
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COS Cells
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Chlorocebus aethiops
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DNA-Binding Proteins / biosynthesis*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Gene Expression Regulation*
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Homeodomain Proteins
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Humans
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Immunoglobulin J Recombination Signal Sequence-Binding Protein
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Membrane Proteins / metabolism
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Nuclear Proteins / biosynthesis*
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Nuclear Proteins / genetics
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Promoter Regions, Genetic
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Protein Structure, Tertiary / genetics
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Protein Structure, Tertiary / physiology
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RNA-Binding Proteins
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Receptors, Notch
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Signal Transduction / genetics
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Signal Transduction / physiology*
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Transcription, Genetic / physiology*
Substances
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APBA1 protein, human
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Adaptor Proteins, Signal Transducing
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DNA-Binding Proteins
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Homeodomain Proteins
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Immunoglobulin J Recombination Signal Sequence-Binding Protein
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MSX2 protein
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Membrane Proteins
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Nerve Tissue Proteins
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Nuclear Proteins
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RBPJ protein, human
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RNA-Binding Proteins
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Receptors, Notch
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Spen protein, mouse