| First Author | Xu Y | Year | 1997 |
| Journal | J Biol Chem | Volume | 272 |
| Issue | 21 | Pages | 13463-6 |
| PubMed ID | 9153187 | Mgi Jnum | J:40488 |
| Mgi Id | MGI:87833 | Doi | 10.1074/jbc.272.21.13463 |
| Citation | Xu Y, et al. (1997) Interaction of the adaptor protein Shc and the adhesion molecule cadherin. J Biol Chem 272(21):13463-6 |
| abstractText | In mitogenic signaling pathways, Shc participates in the growth factor activation of Ras by interacting with activated receptors and/or the Grb-2.Sos complex. Using several experimental approaches we demonstrate that Shc, through its SH2 domain, forms a complex with the cytoplasmic domain of cadherin, a transmembrane protein involved in the Ca2+-dependent regulation of cell-cell adhesion. This interaction is demonstrated in a yeast two-hybrid assay, by co-precipitation from mammalian cells, and by direct biochemical analysis in vitro. The Shc-cadherin association is phosphotyrosine-dependent and is abrogated by addition of epidermal growth factor to A-431 cells maintained in Ca2+-free medium, a condition that promotes changes in cell shape. Shc may therefore participate in the control of cell-cell adhesion as well as mitogenic signaling through Ras. |
