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XB-ART-9437
Mol Cell Biol 2001 Mar 01;215:1866-73. doi: 10.1128/MCB.21.5.1866-1873.2001.
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Inhibition of Tcf3 binding by I-mfa domain proteins.

Snider L , Thirlwell H , Miller JR , Moon RT , Groudine M , Tapscott SJ .


Abstract
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.

PubMed ID: 11238923
PMC ID: PMC86756
Article link: Mol Cell Biol
Grant support: [+]

Species referenced: Xenopus
Genes referenced: mdfic nodal3.1 nodal3.2 sia1 tcf3 tcf7l1

References [+] :
Behrens, Functional interaction of beta-catenin with the transcription factor LEF-1. 1996, Pubmed, Xenbase