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Mechanistic insights from structural studies of β-catenin and its binding partners
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| Zeitschriftentitel: | Journal of Cell Science |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Cell Science, 120, 2007, 19, S. 3337-3344 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Xu, Wenqing Kimelman, David Xu, Wenqing Kimelman, David |
|---|---|
| author |
Xu, Wenqing Kimelman, David |
| spellingShingle |
Xu, Wenqing Kimelman, David Journal of Cell Science Mechanistic insights from structural studies of β-catenin and its binding partners Cell Biology |
| author_sort |
xu, wenqing |
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Xu, Wenqing Kimelman, David 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.013771 <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> Mechanistic insights from structural studies of β-catenin and its binding partners Journal of Cell Science |
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Journal of Cell Science |
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| title |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_unstemmed |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_full |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_fullStr |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_full_unstemmed |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_short |
Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_sort |
mechanistic insights from structural studies of β-catenin and its binding partners |
| topic |
Cell Biology |
| url |
http://dx.doi.org/10.1242/jcs.013771 |
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2007 |
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3337-3344 |
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<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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| description | <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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| series | Journal of Cell Science |
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| spelling | Xu, Wenqing Kimelman, David 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.013771 <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> Mechanistic insights from structural studies of β-catenin and its binding partners Journal of Cell Science |
| spellingShingle | Xu, Wenqing, Kimelman, David, Journal of Cell Science, Mechanistic insights from structural studies of β-catenin and its binding partners, Cell Biology |
| title | Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_full | Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_fullStr | Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_full_unstemmed | Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_short | Mechanistic insights from structural studies of β-catenin and its binding partners |
| title_sort | mechanistic insights from structural studies of β-catenin and its binding partners |
| title_unstemmed | Mechanistic insights from structural studies of β-catenin and its binding partners |
| topic | Cell Biology |
| url | http://dx.doi.org/10.1242/jcs.013771 |