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  • Title: p120-independent modulation of E-cadherin adhesion activity by the membrane-proximal region of the cytoplasmic domain.
    Author: Ozawa M.
    Journal: J Biol Chem; 2003 Nov 14; 278(46):46014-20. PubMed ID: 12952959.
    Abstract:
    Cadherins are transmembrane glycoproteins that function as Ca2+-dependent cell-cell adhesion molecules and are linked to the actin cytoskeleton via catenins. Previously, we showed that, although E-cadherin lacking its cytoplasmic tail is active in aggregation assays, partially truncated E-cadherin lacking the carboxyl-terminal catenin-binding site is not. Contrary to this observation, a similar N-cadherin construct is found to be functional. Chimeric constructs, in which the membrane-proximal region of the partially truncated E-cadherin was replaced by that of N-cadherin, are active in aggregation assays. N-cadherin constructs in the opposite manner are nonfunctional. Although deletion of the membrane-proximal region, which eliminates the binding site for p120, results in activation of the nonfunctional E-cadherin mutant polypeptides, amino acid substitutions in the membrane-proximal region, which uncouple p120 binding, do not. The p120 uncoupling could not activate a full-length E-cadherin construct, which was beta-catenin-uncoupled by amino acid substitutions in the catenin-binding site. These results indicate that the membrane-proximal region determines the activity of these cadherin constructs but that p120 does not seem directly involved in the modulation of E-cadherin activity.
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