Na. Chitaev et Sm. Troyanovsky, ADHESIVE BUT NOT LATERAL E-CADHERIN COMPLEXES REQUIRE CALCIUM AND CATENINS FOR THEIR FORMATION, The Journal of cell biology, 142(3), 1998, pp. 837-846
We examined intercadherin interactions in epithelial A-431 cells produ
cing endogenous E-cadherin and recombinant forms of E-cadherin tagged
either by myc or by flag epitopes. Three distinct E-cadherin complexes
were found. The first is a conventional E-cadherin-catenin complex co
nsisting of one E-cadherin molecule linked either to beta-catenin/alph
a-catenin or to plakoglobin/alpha-catenin dimers. The second is a late
ral E-cadherin complex incorporating two E-cadherin-catenin convention
al complexes combined in parallel fashion via dimerization of the NH2-
terminal extracellular domain of E-cadherin, The third complex is like
ly to contain two E-cadherin-catenin conventional complexes derived fr
om two opposing cells and arranged in an antiparallel fashion. Formati
on of the antiparallel but not lateral complex strictly depends on ext
racellular calcium and E-cadherin binding to catenins, Double amino ac
id substitution Trp156Ala/Val157Gly within the extracellular NH2-termi
nal E-cadherin domain completely abolished both lateral and antiparall
el inter-E-cadherin association. These data support an idea that the a
ntiparallel complex has the adhesion function. Furthermore, they allow
us to suggest that antiparallel complexes derive from lateral dimers
and this complex process requires catenins and calcium ions.