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- W2095086052 abstract "Beta-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 beta-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 beta-catenin, since it serves as a common binding site for several beta-catenin-binding partners, with steric hindrance limiting which partners can be bound at a specific time. These studies provide important insights into beta-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 beta-catenin expression." @default.
- W2095086052 created "2016-06-24" @default.
- W2095086052 creator A5057871238 @default.
- W2095086052 creator A5085704704 @default.
- W2095086052 date "2007-10-01" @default.
- W2095086052 modified "2023-09-30" @default.
- W2095086052 title "Mechanistic insights from structural studies of β-catenin and its binding partners" @default.
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- W2095086052 doi "https://doi.org/10.1242/jcs.013771" @default.
- W2095086052 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17881495" @default.
- W2095086052 hasPublicationYear "2007" @default.
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