Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts.
Open Access
- 1 August 1992
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 118 (3), 703-714
- https://doi.org/10.1083/jcb.118.3.703
Abstract
Rat 3Y1 cells acquire metastatic potential when transformed with v-src, and this potential is enhanced by double transformation with v-src and v-fos (Taniguchi, S., T. Kawano, T. Mitsudomi, G. Kimura, and T. Baba. 1986. Jpn. J. Cancer Res. 77:1193-1197). We compared the activity of cadherin cell adhesion molecules of normal 3Y1 cells with that of v-src transformed (SR3Y1) and v-src and v-fos double transformed (fosSR3Y1) 3Y1 cells. These cells expressed similar amounts of P-cadherin, and showed similar rates of cadherin-mediated aggregation under suspended conditions. However, the aggregates or colonies of these cells were morphologically distinct. Normal 3Y1 cells formed compacted aggregates in which cells are firmly connected with each other, whereas the transformed cells were more loosely associated, and could freely migrate out of the colonies. Overexpression of exogenous E-cadherin in these transformed cells had no significant effect on their adhesive properties. We then found that herbimycin A, a tyrosine kinase inhibitor, induced tighter cell-cell associations in the aggregates of the transformed cells. In contrast, vanadate, a tyrosine phosphatase inhibitor, inhibited the cadherin-mediated aggregation of SR3Y1 and fosSR3Y1 cells but had little effect on that of normal 3Y1 cells. These results suggest that v-src-mediated tyrosine phosphorylation perturbs cadherin function directly or indirectly, and the inhibition of tyrosine phosphorylation restores cadherin action to the normal state. We next studied tyrosine phosphorylation on cadherins and the cadherin-associated proteins, catenins. While similar amounts of catenins were expressed in all of these cells, the 98-kD catenin was strongly tyrosine phosphorylated only in SR3Y1 and fosSR3Y1 cells. Cadherins were also weakly tyrosine phosphorylated only in the transformed cells. The tyrosine phosphorylation of these proteins was enhanced by vanadate, and inhibited by herbimycin A. Thus, the tyrosine phosphorylation of the cadherin-catenin system itself might affect its function, causing instable cell-cell adhesion.Keywords
This publication has 58 references indexed in Scilit:
- Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor roleCell, 1991
- CADHERINS: A MOLECULAR FAMILY IMPORTANT IN SELECTIVE CELL-CELL ADHESIONAnnual Review of Biochemistry, 1990
- Irreversible inhibition of v-src tyrosine kinase activity by herbimycin a and its abrogation by sulfhydryl compoundsBiochemical and Biophysical Research Communications, 1989
- Expressed recombinant cadherins mediate cell sorting in model systemsCell, 1988
- Malignant progression of a transformed rat cell line by transfer of the v-fos oncogeneBiochemical and Biophysical Research Communications, 1987
- Scatter factor is a fibroblast-derived modulator of epithelial cell mobilityNature, 1987
- Some structural and functional aspects of the cell adhesion molecule uvomorulinCell Differentiation, 1984
- Cleavage stage mouse embryos share a common cell adhesion system with teratocarcinoma cellsDevelopmental Biology, 1982
- Immunological detection of cell surface components related with aggregation of Chinese hamster and chick embryonic cellsDevelopmental Biology, 1979
- Microspike-mediated particle transport towards the cell body during early spreading of 3T3 cellsExperimental Cell Research, 1976