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Tyrosine phosphorylation is a well-conserved mechanism for transmitting extracellular signals inside a cell. Peptide receptor tyrosine kinase (p180-catenin) (also known as p120-catenin, E-cadherin, or catenin p120) is a transmembrane protein that is involved in Wnt signaling and cell-cell adhesion. It also contains a tyrosine kinase domain in its extracellular region. It was initially identified as a component of the adherens junction, a specialized structure that exists between adjacent cells. Catenin p120 is a cytosolic protein that binds to the cytoplasmic region of cadherins. Wnt signaling is known to play critical roles in embryonic development and regulation of cell proliferation. Catenin p120 is known to bind to β-catenin and Axin to form a protein complex that is responsible for the phosphorylation and degradation of β-catenin. In the absence of Wnt signaling, the protein complex is not formed, leading to increased levels of β-catenin. β-catenin is a component of a transcriptional complex that activates the expression of genes including c-myc, cyclin D1, and metalloproteinase (MMP) 7.
p120-catenin is also known to be associated with the AGE-RIK pathway in the regulation of the actin cytoskeleton. Recent studies suggest that modulation of the AGE-RIK pathway is a novel approach for the prevention or treatment of atherosclerosis
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