ArticleMolecular and cellular biology1994
A dominant negative erythropoietin (EPO) receptor inhibits EPO-dependent growth and blocks F-gp55-dependent transformation.
Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 54 citations in OpenAlex.
- The SH2B1 adaptor protein associates with a proximal region of the erythropoietin receptor.The Journal of biological chemistry · 2012Article
- Random mutagenesis reveals residues of JAK2 critical in evading inhibition by a tyrosine kinase inhibitor.PloS one · 2012Article
- The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011Review
- Dominant action of mutated erythropoietin receptors on differentiation in vitro and erythroleukemia development in vivo.Oncogene · 2000Article
- Oligomerization and scaffolding functions of the erythropoietin receptor cytoplasmic tail.The Journal of biological chemistry · 1999Article
- Both the polycythemia- and anemia-inducing strains of Friend spleen focus-forming virus induce constitutive activation of the Raf-1/mitogen-activated protein kinase signal transduction pathway.Journal of virology · 1998Article
- A chimeric receptor/oncogene that can be regulated by a ligand in vitro and in vivo.The Journal of clinical investigation · 1997Article
- Mutation in the Jak kinase JH2 domain hyperactivates Drosophila and mammalian Jak-Stat pathways.Molecular and cellular biology · 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
- A sequential dimerization mechanism for erythropoietin receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Deletions in one domain of the Friend virus-encoded membrane glycoprotein overcome host range restrictions for erythroleukemia.Journal of virology · 1995Article
- Erythropoietin and interleukin-2 activate distinct JAK kinase family members.Molecular and cellular biology · 1994Article
- 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
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The erythropoietin receptor (EPO-R), a member of the cytokine receptor superfamily, can be activated to signal cell growth by binding either EPO or F-gp55, the Friend spleen focus-forming virus glycoprotein. Activation by F-gp55 results in constitutive EPO-R signalling and the first stage of Friend virus-induced erythroleukemia. We have generated a truncated form of the EPO-R polypeptide [EPO-R(T)] which lacks the critical cytoplasmic signal-transducing domain of the EPO-R required for EPO- or F-gp55-induced cell growth. EPO-R(T) specifically inhibited the EPO-dependent growth of EPO-R-expressing Ba/F3 cells without changing the interleukin-3-dependent growth of these cells. In addition, Ba/F3 cells that coexpressed wild-type EPO-R and EPO-R(T) were resistant to transformation by F-gp55 despite efficient expression of the F-gp55 transforming oncoprotein in infected cells. EPO-R(T) inhibited the EPO-dependent tyrosine phosphorylation of wild-type EPO-R, the tyrosine kinase (JAK2), and the SH2 adaptor protein (Shc). In conclusion, the EPO-R(T) polypeptide is a dominant negative polypeptide which specifically interferes with the early stages of EPO-R-mediated signal transduction and which prevents Friend virus transformation of erythroblasts.
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