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© The Rockefeller University Press, 0021-9525/1997//1109 $5.00
The Journal of Cell Biology, Volume 136, Number 5, , 1997 1109-1121

Article

LI-Cadherin–mediated Cell–Cell Adhesion Does Not Require Cytoplasmic Interactions



Bertolt Kreft*, Dietmar Berndorff*, Anja Böttinger*, Silvia Finnemann{ddagger}, Doris Wedlich{ddagger}, Michael Hortsch§, Rudolf Tauber*, and Reinhard Geßner*

* Institute of Clinical Chemistry and Biochemistry, Virchow-Hospital, Humboldt-University Berlin, Germany; {ddagger} Department of Biochemistry, University of Ulm, Germany, § Department of Anatomy and Cell Biology, University of Michigan, Ann Arbor, Michigan 48109

The adhesive function of classical cadherins depends on the association with cytoplasmic proteins, termed catenins, which serve as a link between cadherins and the actin cytoskeleton. LI-cadherin, a structurally different member of the cadherin family, mediates Ca2+-dependent cell–cell adhesion, although its markedly short cytoplasmic domain exhibits no homology to this highly conserved region of classical cadherins. We now examined whether the adhesive function of LI-cadherin depends on the interaction with catenins, the actin cytoskeleton or other cytoplasmic components. In contrast to classical cadherins, LI-cadherin, when expressed in mouse L cells, was neither associated with catenins nor did it induce an upregulation of β-catenin. Consistent with these findings, LI-cadherin was not resistant to detergent extraction and did not induce a reorganization of the actin cytoskeleton. However, LI-cadherin was still able to mediate Ca2+dependent cell–cell adhesion.

To analyze whether this function requires any interaction with proteins other than catenins, a glycosyl phosphatidylinositol–anchored form of LI-cadherin (LI-cadherinGPI) was constructed and expressed in Drosophila S2 cells. The mutant protein was able to induce Ca2+-dependent, homophilic cell–cell adhesion, and its adhesive properties were indistinguishable from those of wild type LI-cadherin. These findings indicate that the adhesive function of LI-cadherin is independent of any interaction with cytoplasmic components, and consequently should not be sensitive to regulatory mechanisms affecting the binding of classical cadherins to catenins and to the cytoskeleton. Thus, we postulate that the adhesive function of LI-cadherin is complementary to that of coexpressed classical cadherins ensuring cell–cell contacts even under conditions that downregulate the function of classical cadherins.

Abbreviations used in this paper: CRD, cross-reacting determinant; GPI, glycosyl phosphatidylinositol; PCMBS, p-chloromercuriphenylsulfonic acid; PI-PLC, phosphatidylinositol-specific phospholipase C.

Please address all correspondence to Dr. R. Geßner, Institut für Klinische Chemie und Biochemie, Virchow-Klinikum der Humboldt-Universität zu Berlin, Augustenberger Platz 1, D-13353 Berlin, Germany. Tel.: 49 30 450 69007. Fax: 49 30 450 69900. E-Mail: gessner{at}ukrv.de


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