The actin binding domain of the epidermal growth factor receptor is required for EGF-stimulated tissue invasion.

Autor: van der Heyden MA; Department of Molecular Cell Biology, Utrecht University, The Netherlands. m_heyden@hubrecht.nl, Van Bergen en Henegouwen PM, de Ruiter N, Verdaasdonk MA, van den Tweel JG, Rijksen G, Boonstra J, Joling P
Jazyk: angličtina
Zdroj: Experimental cell research [Exp Cell Res] 1997 Aug 01; Vol. 234 (2), pp. 521-6.
DOI: 10.1006/excr.1997.3661
Abstrakt: NIH-3T3 fibroblasts expressing epidermal growth factor receptors (EGFRs) lacking the actin binding domain (ABD) were analyzed for their EGF-induced capacity to invade a bone marrow stromal cell (BMSC) monolayer. The fibroblasts display a reduction in the percentage of cytoskeleton-associated EGFRs. Furthermore, EGF-induced tyrosine kinase activity is unaffected by the mutation. Cells expressing the mutant EGFRs hardly invade a BMSC monolayer upon EGF stimulation in contrast to cells expressing wild-type EGFRs. Using the same cells no difference was observed in PDGF-induced invasion, which ligand was as potent in both cell types as EGF was in wild-type cells. Inhibition of both the phosphatidyl inositol-3-kinase (PI-3-K) and lipoxygenase pathways in wild-type cells mimicked the effect of the ABD deletion. Our results point to an important role for the ABD of the EGFR in EGF-induced tissue invasion.
Databáze: MEDLINE