TY - JOUR
T1 - Casein kinase II phosphorylation of E-cadherin increases E-cadherin/β- catenin interaction and strengthens cell-cell adhesion
AU - Lickert, Heiko
AU - Bauer, Andreas
AU - Kemler, Rolf
AU - Stappert, Jörg
PY - 2000/2/18
Y1 - 2000/2/18
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0034681430&partnerID=8YFLogxK
U2 - 10.1074/jbc.275.7.5090
DO - 10.1074/jbc.275.7.5090
M3 - Article
C2 - 10671552
AN - SCOPUS:0034681430
SN - 0021-9258
VL - 275
SP - 5090
EP - 5095
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -