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Originally published In Press as doi:10.1074/jbc.M007189200 on September 19, 2000

J. Biol. Chem., Vol. 275, Issue 50, 39741-39746, December 15, 2000
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Evidence for Heterotypic Interaction between the Receptor Tyrosine Kinases TIE-1 and TIE-2*

Marie B. Marron, David P. Hughes, Michael D. EdgeDagger , Cheryl L. ForderDagger , and Nicholas P. J. Brindle§

From the Department of Surgery, University of Leicester, RKCSB, P. O. Box 65, Leicester LE2 7LX and the Dagger  Cancer and Infection Bioscience Department, AstraZeneca, Alderley Park, Macclesfield, Cheshire SK10 4TG, United Kingdom

The orphan receptor tyrosine kinase Tie-1 is expressed in endothelial cells and is essential for vascular development. Nothing is known about the signaling pathways utilized by this receptor. In this study we have used chimeric receptors composed of the TrkA ectodomain fused to the transmembrane and intracellular domains of Tie-1, or the related receptor Tie-2, to examine Tie-1 signaling capacity. In contrast to TrkA/Tie-2, the Tie-1 chimera was unable to phosphorylate cellular proteins or undergo autophosphorylation. Consistent with this Tie-1 exhibited negligible kinase activity. Co-immunoprecipitation analysis revealed Tie-1 was present in endothelial cells bound to Tie-2. Full-length Tie-1 and truncated receptor, formed by regulated endoproteolytic cleavage, were found to complex with Tie-2. Association was mediated by the intracellular domains of the receptors and did not require Tie-1 to be membrane-localized. Tie-1 bound to Tie-2 was not tyrosine-phosphorylated under basal conditions or following Tie-2 stimulation. This study provides the first evidence for the existence of a pre-formed complex of Tie-1 and Tie-2 in endothelial cells. The data suggest Tie-1 does not signal via ligand-induced kinase activation involving homo-oligomerization. The physical association between Tie-1 and Tie-2 is consistent with Tie-1 having a role in modulating Tie-2 signaling.

* This work was supported by Grant PG97104 from the British Heart Foundation.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.

§ To whom correspondence should be addressed: Dept of Surgery, University of Leicester, RKCSB, P. O. Box 65, Leicester LE2 7LX UK. Tel.: 44-116-252-5802; Fax: 44-116-252-3179; E-mail: npjb1@leicester.ac.uk.

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