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© The Rockefeller University Press,
0021-9525/2000//1161 $5.00
The Journal of Cell Biology, Volume 150, Number 5,
, 2000 1161-1176
Original Article |
Two Cell Adhesion Molecules, Nectin and Cadherin, Interact through Their Cytoplasmic Domain–Associated Proteins
ytakai{at}molbio.med.osaka-u.ac
We have found a new cell–cell adhesion system at cadherin-based cell–cell adherens junctions (AJs) consisting of at least nectin and l-afadin. Nectin is a Ca2+-independent homophilic immunoglobulin-like adhesion molecule, and l-afadin is an actin filament-binding protein that connects the cytoplasmic region of nectin to the actin cytoskeleton. Both the trans-interaction of nectin and the interaction of nectin with l-afadin are necessary for their colocalization with E-cadherin and catenins at AJs. Here, we examined the mechanism of interaction between these two cell–cell adhesion systems at AJs by the use of
-catenin–deficient F9 cell lines and cadherin-deficient L cell lines stably expressing their various components. We showed here that nectin and E-cadherin were colocalized through l-afadin and the COOH-terminal half of
-catenin at AJs. Nectin trans-interacted independently of E-cadherin, and the complex of E-cadherin and
- and β-catenins was recruited to nectin-based cell–cell adhesion sites through l-afadin without the trans-interaction of E-cadherin. Our results indicate that nectin and cadherin interact through their cytoplasmic domain–associated proteins and suggest that these two cell–cell adhesion systems cooperatively organize cell–cell AJs.
Key Words: immunoglobulin superfamily afadin ponsin catenin cell–cell adherens junctions
© 2000 The Rockefeller University Press
Abbreviations used in this paper: aa, amino acid(s); Ab, antibody; AJ, adherens junction; F-actin, actin filament; gD, glycoprotein D; GFP, green fluorescent protein; GST, glutathione-S-transferase; HA, hemagglutinin; His6, hexa-histidine; HSV1, herpes simplex virus type 1; Ig, immunoglobulin; TJ, tight junction.
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