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

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.

journal_name

Mol Cell

journal_title

Molecular cell

authors

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

doi

10.1016/s1097-2765(01)00241-6

subject

Has Abstract

pub_date

2001-05-01 00:00:00

pages

927-36

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00241-6

journal_volume

7

pub_type

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