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J Biol Chem, Vol. 275, Issue 8, 5779-5784, February 25, 2000

Discoidin Domain Receptor 1 Is Activated Independently of beta 1 Integrin*

Wolfgang VogelDagger §, Cord Brakebusch, Reinhard Fässler, Frauke Alves||, Florence Ruggiero**, and Tony PawsonDagger Dagger Dagger §§

From the Dagger  Programme in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada, the  Department of Experimental Pathology, Lund University, 22185 Lund, Sweden, the || Department of Hematology and Oncology, University of Göttingen, 37075 Göttingen, Germany, the ** Institute de Biologie et Chimie des Proteines, CNRS, 69367 Lyon, France, and the Dagger Dagger  Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada

Various types of collagen have been identified as potential ligands for the two mammalian discoidin domain receptor (DDR) tyrosine kinases, DDR1 and DDR2. It is presently unclear whether collagen-induced DDR receptor activation, which occurs with very slow kinetics, involves additional proteins with kinase activity or membrane-anchored proteins serving as coreceptors. In particular, the role of the collagen-binding integrins alpha 1beta 1 or alpha 2beta 1 in the DDR activation process is undefined. Here, we provide three lines of evidence suggesting that DDR1 signaling is distinct from integrin activation. First we demonstrate that the enzymatic activity of DDR1 is essential for receptor tyrosine phosphorylation. Collagen-induced DDR receptor autophosphorylation can be blocked either by a dominant negative mutant or by a preparation of recombinant extracellular domain. Second, we show DDR1 signals independent of the epidermal growth factor (EGF) receptor. In cells that endogenously express both DDR1 and the EGF receptor, stimulation with EGF does not induce DDR activation. Third, we detected full DDR1 activation after collagen stimulation in cells that have been treated with blocking antibodies for alpha 2beta 1 integrin or in cells with a targeted deletion of the beta 1 integrin gene. Finally, we show that overexpression of dominant negative DDR1 in the myoblast cell line C2C12 blocks cellular differentiation and the formation of myofibers.

* This work was supported by grants from the National Cancer Institute of Canada, the Medical Research Council of Canada, the Protein Engineering Network of Centers of Excellence, and by an International Research Scholar Award from the Howard Hughes Medical Institute (to T. P.).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.

§ Recipient of Fellowship Vo 663/1-1 of the Deutsche Forschungsgemeinschaft. Present address and to whom correspondence should be addressed: Georg-Speyer-Haus-Institute for Biomedical Research, affiliated with the J. W. Goethe-University Frankfurt, Paul-Ehrlich-Strasse 42-44 60596 Frankfurt am Main, Germany. Tel.: 49-69-63395-222; Fax: 49-69-63395-297. E-mail: W.Vogel@em.uni-frankfurt.de.

§§ Distinguished Scientist of the Medical Research Council of Canada.

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