Beta-catenin
Beta-catenin is a protein that in humans is encoded by the CTNNB1 gene. This protein is part of a complex of proteins that constitute adherens junctions (AJs). AJs are necessary for the creation and maintenance of epithelial cell layers by regulating cell growth and adhesion between cells. Beta-catenin also anchors the actin cytoskeleton and may be responsible for transmitting the contact inhibition signal that causes cells to stop dividing once the epithelial sheet is complete.
Etymology[edit | edit source]
The term "beta-catenin" is derived from the Greek word "katenin" meaning "down" and the prefix "beta" indicating its position in the sequence of proteins identified in the catenin family.
Structure[edit | edit source]
Beta-catenin is a 781-amino acid protein that contains several functional domains: an N-terminal domain, a C-terminal domain, and a central regulatory domain. The N-terminal domain is involved in the regulation of beta-catenin stability. The C-terminal domain is involved in transactivation and interaction with other proteins. The central regulatory domain contains 12 imperfect repeats known as armadillo repeats.
Function[edit | edit source]
Beta-catenin has dual functions in the cell: cell-cell adhesion and gene transcription. In cell-cell adhesion, beta-catenin forms complexes with cadherin proteins and is linked to the actin cytoskeleton through alpha-catenin. In gene transcription, beta-catenin interacts with TCF/LEF transcription factors to activate the transcription of target genes.
Clinical significance[edit | edit source]
Mutations and overexpression of beta-catenin have been implicated in many cancers, including hepatocellular carcinoma, colorectal carcinoma, lung cancer, ovarian cancer, and endometrial cancer. Beta-catenin is also involved in the development of adenomas and the progression to adenocarcinomas in the colon.
See also[edit | edit source]
References[edit | edit source]
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