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The Actin Binding Domain of the Epidermal Growth Factor Receptor Is Required for EGF-Stimulated Tissue Invasion |
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| Authors: | Marcel A.G. van der Heyden Paul M.P. Van Bergen en Henegouwen Nancy de Ruiter Marina A.M. Verdaasdonk Jan G. van den Tweel Gert Rijksen Johannes Boonstra Piet Joling |
| Affiliation: | aDepartment of Molecular Cell Biology, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands;bDepartment of Pathology, University Hospital, P.O. Box 85.500, 3508 GA, Utrecht, The Netherlands;cDepartment of Haematology, University Hospital, P.O. Box 85.500, 3508 GA, Utrecht, The Netherlands |
| Abstract: | 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. |
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