[HTML][HTML] Identification of Tyrosine Residues in the Intracellular Domain of the Growth Hormone Receptor Required for Transcriptional Signaling and Stat5 Activation (∗ …
LH Hansen, X Wang, JJ Kopchick… - Journal of Biological …, 1996 - ASBMB
The binding of growth hormone (GH) to its receptor results in its dimerization followed by
activation of Jak2 kinase and tyrosine phosphorylation of the GH receptor itself, as well as
Jak2 and the transcription factors Stat1,− 3, and− 5. In order to study the role of GH receptor
tyrosine phosphorylation in intracellular signaling, we constructed GH receptors in which
combinations of tyrosines were mutated to phenylalanines. We identified three tyrosine
residues at positions 534, 566, and 627 that were required for activation of GH-stimulated …
activation of Jak2 kinase and tyrosine phosphorylation of the GH receptor itself, as well as
Jak2 and the transcription factors Stat1,− 3, and− 5. In order to study the role of GH receptor
tyrosine phosphorylation in intracellular signaling, we constructed GH receptors in which
combinations of tyrosines were mutated to phenylalanines. We identified three tyrosine
residues at positions 534, 566, and 627 that were required for activation of GH-stimulated …