ArticleMolecular and cellular biology1992
In vitro phosphorylation of the erythropoietin receptor and an associated protein, pp130.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Targeting low-risk myelodysplastic syndrome with novel therapeutic strategies.Trends in molecular medicine · 2021Review
- SOCS, SPRED, and NR4a: Negative regulators of cytokine signaling and transcription in immune tolerance.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2021Article
- The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011Review
- Phosphorylation of erythropoietin receptors in the endoplasmic reticulum by pervanadate-mediated inhibition of tyrosine phosphatases.The Biochemical journal · 1997Article
- Functional interaction of erythropoietin and stem cell factor receptors is essential for erythroid colony formation.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The beta c component of the granulocyte-macrophage colony-stimulating factor (GM-CSF)/interleukin 3 (IL-3)/IL-5 receptor interacts with a hybrid GM-CSF/erythropoietin receptor to influence proliferation and beta-globin mRNA expression.Molecular medicine (Cambridge, Mass.) · 1996Article
- Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation.The EMBO journal · 1996Article
- A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors.The EMBO journal · 1995Article
- A single phosphotyrosine residue of the prolactin receptor is responsible for activation of gene transcription.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Activated Ki-Ras complements erythropoietin signaling in CTLL-2 cells, inducing tyrosine phosphorylation of a 160-kDa protein.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Activation of JAK2 tyrosine kinase by prolactin receptors in Nb2 cells and mouse mammary gland explants.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Association of the transmembrane TGF-alpha precursor with a protein kinase complex.The Journal of cell biology · 1994Article
- Ligand-induced activation of chimeric receptors between the erythropoietin receptor and receptor tyrosine kinases.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- The erythropoietin receptor: its role in hematopoiesis and myeloproliferative diseases.The Journal of cell biology · 1993Review
- Distinct cytoplasmic regions of the human granulocyte colony-stimulating factor receptor involved in induction of proliferation and maturation.Molecular and cellular biology · 1993Article
- The functional form of the erythropoietin receptor is a 78-kDa protein: correlation with cell surface expression, endocytosis, and phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- The serum response element can mediate induction of c-fos by growth hormone.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Truncated erythropoietin receptor causes dominantly inherited benign human erythrocytosis.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- A Friend virus mutant that overcomes Fv-2rr host resistance encodes a small glycoprotein that dimerizes, is processed to cell surfaces, and specifically activates erythropoietin receptors.Journal of virology · 1993Article
- Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors.Molecular and cellular biology · 1993Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The cytoplasmic domain of the cloned erythropoietin (EPO) receptor (EPOR) contains no protein kinase motif, yet addition of EPO to EPO-responsive cells causes an increase in protein-tyrosine phosphorylation. Here we show that addition of EPO or interleukin-3 (IL-3) to an IL-3-dependent cell line expressing the wild-type EPOR causes a small fraction (less than 5%) of total cellular EPOR to shift in gel mobility from 66 to 72 kDa, due at least in part to phosphorylation. Using biotinylated EPO as an affinity reagent, we show that the 72-kDa species is greatly enriched on the cell surface. To demonstrate that a protein kinase activity associates with cell surface EPOR, cells were incubated with biotinylated EPO and then cross-linked with a thiol-cleavable chemical cross-linker. The avidin-agarose-selected complexes were incubated with [gamma-32P]ATP. After in vitro phosphorylation and denaturation without reducing agent, both antiphosphotyrosine and anti-EPOR antibodies immunoprecipitated labeled 72-kDa EPOR and an unidentified 130-kDa phosphoprotein (pp130), indicating that a protein kinase is associated with cell surface EPOR and that a fraction of the EPOR was phosphorylated on tyrosine residues either in the cells or during the cell-free phosphorylation reaction. Under reducing conditions, the 72-kDa phosphorylated EPOR but not pp130 was immunoprecipitated with an anti-EPOR antibody, suggesting that the pp130 is bound to the EPOR by the thiol-cleavable chemical cross-linker. Previously, we showed that deletion of the 42 carboxy-terminal amino acids of the EPOR allows cells to grow in 1/10 the normal EPO concentration, without affecting receptor number or affinity. Two carboxy-terminal truncated EPO receptors that are hyperresponsive to EPO were poorly phosphorylated during the in vitro reaction, suggesting that the carboxy-terminal region of the EPOR contains a site for phosphorylation or a site for interaction with a protein kinase. Our data suggests that phosphorylation or interaction with a protein kinase in the carboxy-terminal region may down-modulate the proliferative action of the EPOR.
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