Prolactin Receptor Regulates Stat5 Tyrosine Phosphorylation and Nuclear Translocation by Two Separate Pathways
Open Access
- 1 March 1998
- journal article
- Published by Elsevier
- Vol. 273 (13), 7709-7716
- https://doi.org/10.1074/jbc.273.13.7709
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Two Discrete Regions of Interleukin-2 (IL2) Receptor β Independently Mediate IL2 Activation of a PD98059/Rapamycin/Wortmannin-insensitive Stat5a/b Serine KinasePublished by Elsevier ,1997
- An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STATOncogene, 1997
- Stat2 Is a Transcriptional Activator That Requires Sequence-specific Contacts Provided by Stat1 and p48 for Stable Interaction with DNAJournal of Biological Chemistry, 1997
- Comparative study on the phosphotyrosine motifs of different cytokine receptors involved in STAT5 activationFEBS Letters, 1996
- Distinct Tyrosine Residues within the Interleukin-2 Receptor β Chain Drive Signal Transduction Specificity, Redundancy, and DiversityPublished by Elsevier ,1996
- Requirement of Serine Phosphorylation for Formation of STAT-Promoter ComplexesScience, 1995
- Intracellular Tyrosine Residues of the Human Growth Hormone Receptor Are Not Required for the Signaling of Proliferation or Jak-STAT ActivationPublished by Elsevier ,1995
- Specific recruitment of SH-PTP1 to the erythropoietin receptor causes inactivation of JAK2 and termination of proliferative signalsCell, 1995
- Regulation of gene expression by prolactinReviews of physiology, biochemistry and pharmacology, 1993
- A novel family of growth factor receptors: A common binding domain in the growth hormone, prolactin, erythropoietin and IL-6 receptors, and the p75 IL-2 receptor β-chainBiochemical and Biophysical Research Communications, 1989