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Tyrosine phosphorylation and src family kinases control keratinocyte cell–cell adhesion (1998)
| Venue: | J. Cell Biol |
| Citations: | 22 - 1 self |
BibTeX
@ARTICLE{Calautti98tyrosinephosphorylation,
author = {Enzo Calautti and Sara Cabodi and Paul L. Stein and Mechthild Hatzfeld and Nancy Kedersha and G. Paolo Dotto},
title = {Tyrosine phosphorylation and src family kinases control keratinocyte cell–cell adhesion},
journal = {J. Cell Biol},
year = {1998}
}
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Abstract
Abstract. In their progression from the basal to upper differentiated layers of the epidermis, keratinocytes undergo significant structural changes, including establishment of close intercellular contacts. An important but so far unexplored question is how these early structural events are related to the biochemical pathways that trigger differentiation. We show here that �-catenin, �-catenin/plakoglobin, and p120-Cas are all significantly tyrosine phosphorylated in primary mouse keratinocytes induced to differentiate by calcium, with a time course similar to that of cell junction formation. Together with these changes, there is an increased association of �-catenin and p120-Cas with E-cadherin, which is prevented by tyrosine kinase inhibition. Treatment of E-cadherin complexes with tyrosine-specific
Keyphrases
tyrosine phosphorylation keratinocyte cell cell adhesion src family kinase early structural event e-cadherin complex catenin plakoglobin undergo significant structural change differentiated layer time course biochemical pathway increased association tyrosine kinase inhibition unexplored question cell junction formation primary mouse keratinocytes close intercellular contact
