Casein Kinase II Phosphorylation of E-cadherin Increases E-cadherin/β-Catenin Interaction and Strengthens Cell-Cell Adhesion*
By Heiko Lickert, A. Bauer, R. Kemler, J. Stappert. Journal of Biological Chemistry, 2000
185 citations recorded by the source corpus.
β-Catenin, a member of the Armadillo repeat protein family, binds directly to the cytoplasmic domain of E-cadherin, linking it via α-catenin to the actin cytoskeleton. A 30-amino acid region within the cytoplasmic domain of E-cadherin, conserved among all classical cadherins, has been shown to be essential for β-catenin binding. This region harbors several putative casein kinase II (CKII) and glycogen synthase kinase-3β (GSK-3β) phosphorylation sites and is highly phosphorylated. Here we report that in vitro this region is indeed phosphorylated by CKII and GSK-3β, which results in an increased binding of β-catenin to E-cadherin. Additionally, in mouse NIH3T3 fibroblasts expression of E-cadherin with mutations in putative CKII sites resulted in reduced cell-cell contacts. Thus, phosphorylation of the E-cadherin cytoplasmic domain by CKII and GSK-3β appears to modulate the affinity between β-catenin and E-cadherin, ultimately modifying the strength of cell-cell adhesion.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/db98819de79a5b6cfb8ce01fa0b0629e30aa4812
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Citations in the corpus
- Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development. (2002, background): “Indeed, phosphorylation of cadherin in vitro increases its ability to bind to -catenin (265), raising the possibility that the cadherin-mediated cell adhesiveness can be regulated by the extent of its -catenin binding.”
- Phosphorylation: Implications in Cancer (2017, background): “1 3 has been reported that in transfected mouse NIH3T3 fibroblasts, by preventing phosphorylation E-cadherin-mediated cell–cell adhesion can be reduced [44].”
- Intercellular adhesion, signalling and the cytoskeleton (2002, background): “, which increases its binding to β-catenin in vitro”
- The cadherin-catenin adhesion system in signaling and cancer. (2002, background): “tion of AJ assembly may also be achieved via phosphorylation by CKII on serine residues of the cadherin cytoplasmic tail, a modification that enhances its binding to β-catenin (44).”