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J. Biol. Chem., Vol. 269, Issue 48, 30154-30157, Dec, 1994
A Pandey, DF Lazar, AR Saltiel and VM Dixit
The Eph/Eck subfamily of receptor protein tyrosine kinases is currently the
largest subfamily of receptor protein tyrosine kinases with a dozen members
(Van der Geer, P., Hunter, T., and Lindberg, R. A. (1994) Annu. Rev. Cell
Biol. 10, 251-337). Using the cytoplasmic domain of Eck as bait in a yeast
two-hybrid screen of mouse embryonic and T-cell cDNA libraries, it was
discovered that the p85 subunit of phosphatidylinositol 3-kinase bound Eck.
Further, using glutathione S- transferase fusion proteins, it was found
that the C-terminal src homology 2 domain of the p85 subunit specifically
interacted with Eck. Additionally, Eck coimmunoprecipitated with p85 in
ligand activated cells confirming their interaction in vivo. In keeping
with the above observations, activation of Eck by its ligand, B61,
increased phosphatidylinositol 3-kinase activity. This is the first
description of a signal transduction pathway initiated by any member of the
Eph/Eck family.
Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity
Department of Pathology, University of Michigan Medical School, Ann Arbor 48109-0602.
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