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

Akhilesh Pandey, Dan F. Lazar, Alan R. Saltiel, Vishva M. Dixit

Research output: Contribution to journalArticlepeer-review

133 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)30154-30157
Number of pages4
JournalJournal of Biological Chemistry
Volume269
Issue number48
StatePublished - Dec 2 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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