| First Author | Masuda Y | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 7 | Pages | 5331-8 |
| PubMed ID | 11084035 | Mgi Jnum | J:67230 |
| Mgi Id | MGI:1930091 | Doi | 10.1074/jbc.M008590200 |
| Citation | Masuda Y, et al. (2001) Dlxin-1, a novel protein that binds Dlx5 and regulates its transcriptional function. J Biol Chem 276(7):5331-8 |
| abstractText | Dlx5, a member of the Dlx family of homeodomain proteins, plays a critical role in bone development and fracture healing. To understand the molecular mechanism underlying the transcriptional regulation by Dlx5, we performed yeast two-hybrid screening and isolated a novel protein, Dlxin-1, that binds Dlx5 and regulates its transcriptional function. Dlxin-1 cDNA encodes a 775-amino acid protein that has a partial homology with necdin at the C terminus and 25 repeats of hexapeptides (WQXPXX) in the middle region. Dlxin-1 mRNA is expressed in various adult tissues, but not the spleen, and also in osteoblastic and chondrogenic cell lines. During embryogenesis, a strong signal for Dlxin-1 mRNA was found in cell layers surrounding cartilaginous elements in bone rudiment during digit formation. Dlxin-1 binds not only Dlx5 but also Dlx7 and Msx2 and forms homomultimers in vivo. Transfection and reporter gene assays indicate that Dlxin-1 activates the transcriptional function of Dlx5. Therefore, Dlxin-1 may act as a regulator of the function of Dlx family members in bone formation. |
