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Publication : Inhibition of Tcf3 binding by I-mfa domain proteins.

First Author  Snider L Year  2001
Journal  Mol Cell Biol Volume  21
Issue  5 Pages  1866-73
PubMed ID  11238923 Mgi Jnum  J:159083
Mgi Id  MGI:4441142 Doi  10.1128/MCB.21.5.1866-1873.2001
Citation  Snider L, et al. (2001) Inhibition of Tcf3 binding by I-mfa domain proteins. Mol Cell Biol 21(5):1866-73
abstractText  We have determined that I-mfa, an inhibitor of several basic helix-loop-helix (bHLH) proteins, and XIC, a Xenopus ortholog of human I-mf domain-containing protein that shares a highly conserved cysteine-rich C-terminal domain with I-mfa, inhibit the activity and DNA binding of the HMG box transcription factor XTcf3. Ectopic expression of I-mfa or XIC in early Xenopus embryos inhibited dorsal axis specification, the expression of the Tcf3/beta-catenin-regulated genes siamois and Xnr3, and the ability of beta-catenin to activate reporter constructs driven by Lef/Tcf binding sites. I-mfa domain proteins can regulate both the Wnt signaling pathway and a subset of bHLH proteins, possibly coordinating the activities of these two critical developmental pathways.
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