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Originally published In Press as doi:10.1074/jbc.C000028200 on March 15, 2000
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J Biol Chem, Vol. 275, Issue 20, 14783-14786, May 19, 2000

ACCELERATED PUBLICATION
Integrin-mediated RON Growth Factor Receptor Phosphorylation Requires Tyrosine Kinase Activity of Both the Receptor and c-Src*

Alla Danilkovitch-MiagkovaDagger , Debora Angeloni, Alison Skeel, Shannon Donley, Michael Lerman, and Edward J. Leonard

From the Laboratory of Immunobiology, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702

Cooperation between integrins and growth factor receptors plays an important role in the regulation of cell growth, differentiation, and survival. The function of growth factor receptor tyrosine kinases (RTKs) can be regulated by cell adhesion to extracellular matrix (ECM) even in the absence of ligand. We investigated the pathway involved in integrin-mediated RTK activation, using RON, the receptor for macrophage-stimulating protein. Adhesion of RON-expressing epithelial cells to ECM caused phosphorylation of RON, which depended on the kinase activity of both RON itself and c-Src. This conclusion is based on these observations: 1) ECM-induced RON phosphorylation was inhibited in cells expressing kinase-inactive c-Src; 2) active c-Src could phosphorylate immunoprecipitated RON from ECM-stimulated cells but not from unstimulated cells; and 3) ECM did not cause RON phosphorylation in cells expressing kinase-dead RON, nor could active c-Src phosphorylate RON immunoprecipitated from these cells. The data fit a pathway in which ECM-induced integrin aggregation causes both c-Src activation and RON oligomerization followed by RON kinase-dependent autophosphorylation; this results in RON becoming a target for activated c-Src, which phosphorylates additional tyrosines on RON. Integrin-induced epidermal growth factor receptor (EGFR) phosphorylation also depended on both EGFR and c-Src kinase activities. This sequence appears to be a general pathway for integrin-dependent growth factor RTK activation.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Laboratory of Immunobiology, Bldg. 560, Rm. 1246, NCI-Frederick Cancer Research and Development Center, Frederick, MD 21702. Tel.: 301-846-1560; Fax: 301-846-6145; E-mail: danilkovitch@mail.ncifcrf.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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