| First Author | Julius MA | Year | 1999 |
| Journal | Oncogene | Volume | 18 |
| Issue | 1 | Pages | 149-56 |
| PubMed ID | 9926929 | Mgi Jnum | J:52377 |
| Mgi Id | MGI:1329217 | Doi | 10.1038/sj.onc.1202268 |
| Citation | Julius MA, et al. (1999) Chimeric Wnt proteins define the amino-terminus of Wnt-1 as a transformation-specific determinant. Oncogene 18(1):149-56 |
| abstractText | Wnt-1 induces morphological transformation of C57MG mammary epithelial cells and accumulation of cytosolic beta-catenin whereas Wnt-5a has no effect. To identify regions within the 370 amino acid Wnt-1 protein required for these functions we tested eleven chimeric genes that contained variable amounts of Wnt-1 and Wnt-5a sequence. Transformation and beta-catenin regulation in C57MG cells is controlled by amino acids that lie within 186 residues of the amino terminus of Wnt-1. Small substitutions between residues 186 and 292 reduced Wnt-1 activity. Replacement of the carboxy terminal 79 amino acids of Wnt-1 by Wnt-5a did not affect function. These results were supported by transient expression assays in 293 cells wherein beta-catenin accumulated in the cytoplasm in response to ectopic Wnt-1 expression. In 293 cells, a larger region of the amino-terminus of Wnt-1 was found to be required for beta-catenin regulation. Nonfunctional chimeras that contained at least 99 amino terminal Wnt-1 residues inhibited Wnt-1 stimulation of 293 cells. One of these chimeras inhibited both Wnt-1 and Wnt-3 activity suggesting that Wnt-1 and Wnt-3 interact with a common signaling component. |
