Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses
- PMID: 11389839
- DOI: 10.1016/s1097-2765(01)00242-8
Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses
Abstract
Destruction of beta-catenin is regulated through phosphorylation-dependent interactions with the F box protein beta-TrCP. A novel pathway for beta-catenin degradation was discovered involving mammalian homologs of Drosophila Sina (Siah), which bind ubiquitin-conjugating enzymes, and Ebi, an F box protein that binds beta-catenin independent of the phosphorylation sites recognized by beta-TrCP. A series of protein interactions were identified in which Siah is physically linked to Ebi by association with a novel Sgt1 homolog SIP that binds Skp1, a central component of Skp1-Cullin-F box complexes. Expression of Siah is induced by p53, revealing a way of linking genotoxic injury to destruction of beta-catenin, thus reducing activity of Tcf/LEF transcription factors and contributing to cell cycle arrest.
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