| First Author | Li J | Year | 2005 |
| Journal | Biochim Biophys Acta | Volume | 1729 |
| Issue | 1 | Pages | 50-6 |
| PubMed ID | 15777657 | Mgi Jnum | J:100083 |
| Mgi Id | MGI:3586927 | Doi | 10.1016/j.bbaexp.2005.02.001 |
| Citation | Li J, et al. (2005) The C terminus of MINT forms homodimers and abrogates MINT-mediated transcriptional repression. Biochim Biophys Acta 1729(1):50-6 |
| abstractText | 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. |
