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XB-ART-8950
Mol Cell. May 1, 2001; 7 (5): 927-36.

Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein.

Liu J , Stevens J , Rote CA , Yost HJ , Hu Y , Neufeld KL , White RL , Matsunami N .


Abstract
The adenomatous polyposis coli (APC) tumor-suppressor protein, together with Axin and GSK3beta, forms a Wnt-regulated signaling complex that mediates phosphorylation-dependent degradation of beta-catenin by the proteasome. Siah-1, the human homolog of Drosophila seven in absentia, is a p53-inducible mediator of cell cycle arrest, tumor suppression, and apoptosis. We have now found that Siah-1 interacts with the carboxyl terminus of APC and promotes degradation of beta-catenin in mammalian cells. The ability of Siah-1 to downregulate beta-catenin signaling was also demonstrated by hypodorsalization of Xenopus embryos. Unexpectedly, degradation of beta-catenin by Siah-1 was independent of GSK3beta-mediated phosphorylation and did not require the F box protein beta-TrCP. These results indicate that APC and Siah-1 mediate a novel beta-catenin degradation pathway linking p53 activation to cell cycle control.

PubMed ID: 11389840
Article link: Mol Cell.
Grant support: 5PO1 CA73992-02 NCI NIH HHS , 5PO1 CA73992-02 NCI NIH HHS , 5PO1 CA73992-02 NCI NIH HHS , 5PO1 CA73992-02 NCI NIH HHS , 5PO1 CA73992-02 NCI NIH HHS , 5PO1 CA73992-02 NCI NIH HHS

Genes referenced: btrc gsk3b siah1 tp53
Antibodies referenced:
Morpholinos referenced:

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