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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tauber, R. Kreft, B. Böttinger, A. Hortsch, M. Gessner, R. Finnemann, S. Berndorff, D. Wedlich, D. |
| Description | Author Affiliation: Kreft B ( Institute of Clinical Chemistry and Biochemistry, Humboldt-University Berlin, Germany.) |
| Abstract | 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 $Ca^{2+}-dependent$ 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 $Ca^{2+}dependent$ cell–cell adhesion. To analyze whether this function requires any interaction with proteins other than catenins, a glycosyl phosphatidylinositol–anchored form of LI-cadherin $(LI-cadherin^{GPI})$ was constructed and expressed in Drosophila S2 cells. The mutant protein was able to induce $Ca^{2+}-dependent,$ 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. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 5 |
| Volume Number | 136 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1997-03-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cadherins Metabolism Carrier Proteins Cell Adhesion Physiology Cytoplasm Membrane Transport Proteins Trans-Activators Actins Amino Acid Sequence Animals Genetics Cell Line Cell Membrane Chemistry Cytoskeletal Proteins Cytoskeleton Drosophila Gene Expression Glycosylphosphatidylinositols L Cells (Cell Line) Mice Molecular Sequence Data Phosphatidylinositol Diacylglycerol-Lyase Phosphoric Diester Hydrolases Pharmacology Transfection Beta Catenin Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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