Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses.

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.
Mesh Terms:
Amino Acid Sequence, Calcium-Binding Proteins, Carrier Proteins, Cell Cycle, Cell Cycle Proteins, Cytoskeletal Proteins, DNA Damage, DNA-Binding Proteins, Drosophila Proteins, GTP-Binding Proteins, Heat-Shock Proteins, Humans, Insect Proteins, Lymphoid Enhancer-Binding Factor 1, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Sequence Alignment, Signal Transduction, Trans-Activators, Transcription Factors, Tumor Cells, Cultured, Tumor Suppressor Protein p53, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases, beta Catenin
Mol. Cell
Date: May. 01, 2001
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