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© The Rockefeller University Press, 0021-9525/2000//579 $5.00
The Journal of Cell Biology, Volume 148, Number 3, , 2000 579-590

Original Article

Functional Cis-Heterodimers of N- and R-Cadherins



Wei-Song Shana, Hidekazu Tanakaa, Greg R. Phillipsa, Kirsten Arndta, Mika Yoshidaa, David R. Colmana, and Lawrence Shapirob

a Department of Biochemistry and Molecular Biology, Programs in Cell Adhesion and Structural Biology
b Department of Physiology and Biophysics, The Mount Sinai School of Medicine of New York University, New York, New York 10029
Structural Biology Program, Department of Physiology and Biophysics, The Mount Sinai School of Medicine, 1425 Madison Avenue, NY, NY 10029.(212) 849-2456(212) 659-8651

shapiro{at}anguilla.physbio.mssm.edu

Classical cadherins form parallel cis-dimers that emanate from a single cell surface. It is thought that the cis-dimeric form is active in cell–cell adhesion, whereas cadherin monomers are likely to be inactive. Currently, cis-dimers have been shown to exist only between cadherins of the same type. Here, we show the specific formation of cis-heterodimers between N- and R-cadherins. E-cadherin cannot participate in these complexes. Cells coexpressing N- and R-cadherins show homophilic adhesion in which these proteins coassociate at cell–cell interfaces. We performed site- directed mutagenesis studies, the results of which support the strand dimer model for cis-dimerization. Furthermore, we show that when N- and R-cadherins are coexpressed in neurons in vitro, the two cadherins colocalize at certain neural synapses, implying biological relevance for these complexes. The present study provides a novel paradigm for cadherin interaction whereby selective cis-heterodimer formation may generate new functional units to mediate cell–cell adhesion.

Key Words: cadherins • cell adhesion • heterophilic binding • synaptic adhesion • dimerization

© 2000 The Rockefeller University Press

Abbreviations used in this paper: DiI, 1,1-dioctadecyl-3,3,3,3-tetramethylindocarbocyanine; DiO, 3,3-dioctadecyloxacarbocyanine perchlorate; EC1, first extracellular domain; GFP, green fluorescence protein; Trp-2, tryptophan 2.


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