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J. Biol. Chem., Vol. 278, Issue 46, 46014-46020, November 14, 2003

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p120-independent Modulation of E-cadherin Adhesion Activity by the Membrane-proximal Region of the Cytoplasmic Domain^*

Masayuki Ozawa

From the Department of Biochemistry and Molecular Biology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan

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 -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.

Received for publication, July 18, 2003 , and in revised form, August 19, 2003.

^* This work was supported by a grant from the Ministry of Education, Culture, Sports, Science and Technology of Japan, a grant-in aid for Science Research on Priority Area (B). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 81-99-275-5928; Fax: 81-99-264-5618; E-mail: mozawa{at}m.kufm.kagoshima-u.ac.jp.

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