| First Author | Ishiguro A | Year | 2004 |
| Journal | Biochem Biophys Res Commun | Volume | 324 |
| Issue | 1 | Pages | 302-7 |
| PubMed ID | 15465018 | Mgi Jnum | J:93136 |
| Mgi Id | MGI:3056015 | Doi | 10.1016/j.bbrc.2004.09.052 |
| Citation | Ishiguro A, et al. (2004) Molecular properties of Zic4 and Zic5 proteins: functional diversity within Zic family. Biochem Biophys Res Commun 324(1):302-7 |
| abstractText | The Zic-family proteins control various developmental processes. Previous studies have shown that Zic1, Zic2, and Zic3 can act as transcriptional regulators, and that their functions are repressed by I-mfa, which has been identified as a repressor for basic helix-loop-helix-type transcriptional factors. Here, we investigated the molecular properties of the Zic4 and Zic5 proteins. Zic4/Zic5 showed DNA-binding activity to the Gli-binding sequence, similar to Zic1/Zic2/Zic3 proteins. However, Zic4/Zic5 did not exhibit any significant transcriptional activation ability nor they bind to I-mfa differently from Zic1/Zic2/Zic3. The nuclear localization of Zic4/Zic5 was not affected by the presence of the I-mfa protein, whereas the Zic1/Zic2/Zic3 proteins were translocated to the cytoplasmic compartment in the presence of I-mfa. The difference may be attributable to the dissimilarity of the N-terminal region between the Zic1/Zic2/Zic3 and Zic4/Zic5 proteins, since the binding of the Zic1/Zic2/Zic3 proteins to I-mfa occurs through their N-terminal regions. |
