Erythropoietin-induced recruitment of Shc via a receptor phosphotyrosine-independent, Jak2-associated pathway.

Academic Article


  • Based on the recently implicated role of Shc as a signaling effector for type I cytokine receptors, factors which mediate the recruitment and phosphorylation of Shc in the erythropoietin receptor (EPOR) system have been studied. FDC-P1 cells stably expressing the wild type murine EPOR supported the EPO-induced association of Shc with Jak2 and its rapid tyrosine phosphorylation. However, this did not depend upon the presence of phosphotyrosine sites within the EPOR and was mediated by a mitogenically deficient receptor form (EPOR329) lacking cytoplasmic tyrosine residues. This was shown both by Western blotting of Shc and Jak2 co-immunoprecipitates and through the development of an in vitro assay for cytokine-induced Shc phosphorylation. The direct association of Shc with Jak2 also was observed and was shown to depend upon EPO-exposure and the SH2 subdomain of Shc. Together, these studies indicate that Jak2, in part, may mediate the EPO-induced phosphorylation of Shc.
  • Authors

  • He, TC
  • Jiang, N
  • Zhuang, H
  • Wojchowski, Don
  • Status

    Publication Date

  • May 12, 1995
  • Published In


  • Animals
  • Base Sequence
  • Blotting, Western
  • Cell Division
  • Cell Line
  • DNA Primers
  • Enzyme Activation
  • Erythropoietin
  • Granulocyte-Macrophage Colony-Stimulating Factor
  • Interleukin-3
  • Janus Kinase 2
  • Molecular Sequence Data
  • Phosphorylation
  • Phosphotyrosine
  • Polymerase Chain Reaction
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Receptors, Erythropoietin
  • Tyrosine
  • Digital Object Identifier (doi)

    Pubmed Id

  • 7538110
  • Start Page

  • 11055
  • End Page

  • 11061
  • Volume

  • 270
  • Issue

  • 19