Adhesion

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Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

1. Reynolds, A.B. and Roczniak-Ferguson, A. (2004) Oncogene 23, 7947-7956.
2. Davis, M. A. et al. (2003) J. Cell Biol. 163, 525-534.
3. Thoreson, M.A. and Reynolds, A.B. (2002) Differentiation 70, 583-589.
4. Anastasiadis, P.Z. and Reynolds, A.B. (2000) J. Cell Sci. 113, 1319-1334.

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Catenin δ-1 Antibody

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