The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin

被引:631
作者
Huber, AH [1 ]
Weis, WI [1 ]
机构
[1] Stanford Univ, Sch Med, Dept Struct Biol & Mol & Cellular Physiol, Stanford, CA 94305 USA
关键词
D O I
10.1016/S0092-8674(01)00330-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:391 / 402
页数:12
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