Tyrosine residues within the intracellular domain of the erythropoietin receptor mediate activation of AP-1 transcription factors.

The Journal of Biological Chemistry
S BergelsonH F Lodish

Abstract

Binding of erythropoietin (Epo) to the Epo receptor (EpoR) initiates a signaling cascade resulting in tyrosine phosphorylation of several proteins and induction of AP-1 transcription factor(s). While Epo is known to activate c-fos gene expression, the mechanism of AP-1 activation is unknown. Here we show that AP-1 activation by Epo requires tyrosine kinase activity and also de novo protein synthesis. Using a mutant EpoR containing no cytosolic tyrosine residues, and a set of eight mutants containing a single cytosolic tyrosine residue, we show that multiple EpoR tyrosines, thought to activate multiple intracellular signal transduction proteins, can mediate AP-1 activation. An EpoR containing only tyrosine 343 or tyrosine 464 supports a maximal level of AP-1 activation. We also show that AP-1 activation does not require maximal STAT5 activation and may occur via a STAT5-independent signaling pathway.

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Citations

Apr 7, 2006·Archives of Pharmacal Research·Seu Run SeongJin Tae Hong
May 14, 1999·Trends in Endocrinology and Metabolism : TEM·S N ConstantinescuH F Lodish
Dec 3, 1999·The International Journal of Biochemistry & Cell Biology·S K Ruscetti
Oct 25, 2002·Journal of Interferon & Cytokine Research : the Official Journal of the International Society for Interferon and Cytokine Research·Armin G Jegalian, Hong Wu
Nov 8, 2001·Proceedings of the National Academy of Sciences of the United States of America·G M Edelman, J A Gally
Nov 3, 2010·American Journal of Physiology. Lung Cellular and Molecular Physiology·Yoshihiko IkedaJoel Moss
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Aug 16, 2000·The Journal of Biological Chemistry·Y YamamuraH F Lodish

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