E-CADHERIN ENGAGEMENT STIMULATES TYROSINE PHOSPHORYLATION

Citation
Ms. Kinch et al., E-CADHERIN ENGAGEMENT STIMULATES TYROSINE PHOSPHORYLATION, Cell adhesion and communication, 4(6), 1996, pp. 425-437
Citations number
51
Categorie Soggetti
Cell Biology",Biology
ISSN journal
10615385
Volume
4
Issue
6
Year of publication
1996
Pages
425 - 437
Database
ISI
SICI code
1061-5385(1996)4:6<425:EESTP>2.0.ZU;2-E
Abstract
Cadherins are cell adhesion molecules concentrated at intercellular ad herens junctions, where they form a multiprotein complex with cytoplas mic catenins. Although cell-cell interactions affect many aspects of c ell behavior, little is known about signaling pathways triggered by ca dherin engagement. We show here that E-cadherin-mediated cell-cell adh esion leads to a rapid increase in tyrosine phosphorylation at sites o f cell-cell contact and that this stimulation of tyrosine phosphorylat ion can be mimicked by aggregation of E-cadherin with antibodies. The proteins that become phosphorylated are distinct from those previously shown to be tyrosine phosphorylated in response to integrin-mediated adhesion and include ras-GAP. We also find that E-cadherin-mediated ty rosine phosphorylation is not required for the assembly of adherens-ty pe junctions.