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Mechanistic insights from structural studies of β-catenin and its binding partners
Gespeichert in:
| Zeitschriftentitel: | Journal of Cell Science |
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| Personen und Körperschaften: | , |
| In: | Journal of Cell Science, 120, 2007, 19, S. 3337-3344 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
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| Schlagwörter: |
| Zusammenfassung: | <jats:p>β-catenin is both a crucial regulator of cell adhesion and the central effector of the canonical Wnt signaling pathway. It functions as a protein organizer by interacting with numerous partners at the membrane, in the cytosol, and in the nucleus. Recent structural and biochemical studies have revealed how β-catenin engages in critical protein-protein interactions by using its armadillo repeat region and its N- and C-terminal domains. The groove in the armadillo repeat region is a particularly interesting feature of β-catenin, since it serves as a common binding site for several β-catenin-binding partners, with steric hindrance limiting which partners can be bound at a specific time. These studies provide important insights into β-catenin-mediated mechanisms of cell adhesion and Wnt signaling and suggest potential approaches for the design of therapeutic agents to treat diseases caused by misregulated β-catenin expression.</jats:p> |
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| Umfang: | 3337-3344 |
| ISSN: |
1477-9137
0021-9533 |
| DOI: | 10.1242/jcs.013771 |