期刊
CELL
卷 105, 期 3, 页码 391-402出版社
CELL PRESS
DOI: 10.1016/S0092-8674(01)00330-0
关键词
-
资金
- NIGMS NIH HHS [GM56169] Funding Source: Medline
As a component of adherens junctions and the Wnt signaling pathway, beta -catenin binds cadherins, Tcf family transcription factors, and the tumor suppressor APC. We have determined the crystal structures of both unphosphorylated and phosphorylated E-cadherin cytoplasmic domain complexed with the arm repeat region of beta -catenin. The interaction spans all 12 arm repeats, and features quasi-independent binding regions that include helices which interact with both ends of the arm repeat domain and an extended stretch of 14 residues which closely resembles a portion of XTcf-3. Phosphorylation of E-cadherin results in interactions with a hydrophobic patch of beta -catenin that mimics the binding of an amphipathic XTcf-3 helix. APC contains sequences homologous to the phosphorylated region of cadherin, and is likely to bind similarly.
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