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J Biol Chem, Vol. 274, Issue 43, 30896-30905, October 22, 1999
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From the The Tek/Tie2 receptor tyrosine kinase plays a
pivotal role in vascular and hematopoietic development. To study the
signal transduction pathways that are mediated by this receptor, we
have used the yeast two-hybrid system to identify signaling molecules that associate with the phosphorylated Tek receptor. Using this approach, we demonstrate that five molecules, Grb2, Grb7, Grb14, Shp2,
and the p85 subunit of phosphatidylinositol 3-kinase can interact with
Tek in a phosphotyrosine-dependent manner through their SH2
domains. Mapping of the binding sites of these molecules on Tek reveals
the presence of a multisubstrate docking site in the carboxyl tail of
Tek (Tyr1100). Mutation of this site abrogates
binding of Grb2 and Grb7 to Tek in vivo, and this site is
required for tyrosine phosphorylation of Grb7 and p85 in
vivo. Furthermore, stimulation of Tek-expressing cells with
Angiopoietin-1 results in phosphorylation of both Tek and p85 and in
activation of endothelial cell migration and survival pathways that are
dependent in part on phosphatidylinositol 3-kinase. Taken together,
these results demonstrate that Angiopoietin-1-induced signaling from
the Tek receptor is mediated by a multifunctional docking site that is
responsible for activation of both cell migration and cell survival pathways.
Division of Cancer Biology Research, Amgen Institute, Toronto, Ontario
M5G 2G1, Canada, the ** Molecular/Cancer Biology Laboratory, Haartman
Institute, University of Helsinki, 00014 Helsinki, Finland, the
National Cancer Centre Research Institute,
Tsukiji 5-chome, Chuo-ku, Tokyo, Japan, and the
§§ Cancer Research Program, Garvan Institute of
Medical Research, St. Vincent's Hospital, Sydney, New South Wales
2010, Australia
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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