Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity.

作者:

DOI: 10.1016/S0021-9258(18)43790-8

关键词: Proto-oncogene tyrosine-protein kinase SrcSignal transductionErythropoietin-producing hepatocellular (Eph) receptorReceptor Protein-Tyrosine KinasesMolecular biologyTyrosine kinaseProtein subunitPhosphatidylinositolBiologyKinase activity

摘要: The Eph/Eck subfamily of receptor protein tyrosine kinases is currently the largest with a dozen members (Van der Geer, P., Hunter, T., and Lindberg, R. A. (1994) Annu. Rev. Cell Biol. 10, 251-337). Using cytoplasmic domain Eck as bait in yeast two-hybrid screen mouse embryonic T-cell cDNA libraries, it was discovered that p85 subunit phosphatidylinositol 3-kinase bound Eck. Further, using glutathione S-transferase fusion proteins, found C-terminal src homology 2 specifically interacted Additionally, coimmunoprecipitated ligand activated cells confirming their interaction vivo. In keeping above observations, activation by its ligand, B61, increased activity. This first description signal transduction pathway initiated any member family.

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