Cadherins are transmembrane glycoproteins vital in calcium-dependent cell-cell adhesion during tissue differentiation. Cadherins cluster to form foci of homophilic binding units. A key determinant to the strength of the cadherin-mediated adhesion may be by the juxtamembrane region in cadherins. This region induces clustering and also binds to the protein p120 catenin. The cytoplasmic region is highly conserved in sequence and has been shown experimentally to regulate the cell-cell binding function of the extracellular domain of E-cadherin, possibly through interaction with the cytoskeleton. Many cadherins are regulated by phosphorylation, including N-cadherin and E-cadherin. N-cadherin is phosphorylated by c-Src at Tyr-820, Tyr-853, Tyr-860, Tyr-884, and Tyr-886. Phosphorylation of Tyr-860 (Tyr-835 in E-cadherin) can disrupt cadherin binding to β-catenin. Since many of these tyrosine sites are conserved in the cadherin family, phosphorylation of these sites may be critical for cadherin function.
Qi, J. et al. (2006) Mol. Biol. Cell 17(3):1261.
Xu, Y. et al. (1997) J. Biol. Chem. 272(21):13463.
Takeichi, M. (1988) Development 102:639.
*For more information, see UniProt Accession P12830
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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