Casein kinase II phosphorylation of E-cadherin increases E-cadherin/β- catenin interaction and strengthens cell-cell adhesion

Heiko Lickert, Andreas Bauer, Rolf Kemler, Jörg Stappert

Publikation: Beitrag in FachzeitschriftArtikelBegutachtung

175 Zitate (Scopus)

Abstract

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.

OriginalspracheEnglisch
Seiten (von - bis)5090-5095
Seitenumfang6
FachzeitschriftJournal of Biological Chemistry
Jahrgang275
Ausgabenummer7
DOIs
PublikationsstatusVeröffentlicht - 18 Feb. 2000
Extern publiziertJa

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