| First Author | Sakanaka C | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 20 | Pages | 14090-3 |
| PubMed ID | 10318824 | Mgi Jnum | J:54993 |
| Mgi Id | MGI:1336856 | Doi | 10.1074/jbc.274.20.14090 |
| Citation | Sakanaka C, et al. (1999) Functional domains of axin. Importance of the C terminus as an oligomerization domain. J Biol Chem 274(20):14090-3 |
| abstractText | To understand the mechanism of how Axin acts as an inhibitory molecule in the Wnt pathway, we generated a series of mutated forms of Axin. From the binding experiments, we defined the domains of Axin that bind glycogen synthase kinase-3beta (GSK-3beta) and beta-catenin. We also examined the ability of each Axin mutant to inhibit lymphoid enhancer factor-1 (Lef-1) reporter activity in a cell line expressing high levels of beta-catenin. Axin mutants that did not bind GSK-3beta or beta-catenin were ineffective in suppressing Lef-1 reporter activity. Binding GSK-3beta and beta-catenin was not sufficient for this inhibitory effect of Axin. Axin mutants with C-terminal truncations lacked the ability to inhibit Lef-1 reporter activity, even though they bound GSK-3beta and beta-catenin. The C-terminal region was required for binding to Axin itself. Substitution of the C-terminal region with an unrelated dimerizing molecule, the retinoid X receptor restored its inhibitory effect on Lef-1-dependent transcription. The oligomerization of Axin through its C terminus is important for its function in regulation of beta-catenin-mediated response. |
