期刊
EMBO JOURNAL
卷 19, 期 10, 页码 2270-2279出版社
WILEY
DOI: 10.1093/emboj/19.10.2270
关键词
Axin; adenomatous polyposis coli; crystal structure; regulators of G-protein signaling; Wnt signaling
资金
- NIGMS NIH HHS [R01GM56169, R01 GM056169] Funding Source: Medline
Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3 beta (GSK3 beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily, The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.
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