ArticleProceedings of the National Academy of Sciences of the United States of America1996
A sequential dimerization mechanism for erythropoietin receptor activation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 70 citations in OpenAlex.
- Whether Erythropoietin can be a Neuroprotective Agent against Premature Brain Injury: Cellular Mechanisms and Clinical Efficacy.Current neuropharmacology · 2022Review
- Cell-free protein synthesis as a novel tool for directed glycoengineering of active erythropoietin.Scientific reports · 2018Article
- Alternative Erythropoietin Receptors in the Nervous System.Journal of clinical medicine · 2018Review
- JAK2 activation by growth hormone and other cytokines.The Biochemical journal · 2015Review
- The influence of artificially introduced N-glycosylation sites on the in vitro activity of Xenopus laevis erythropoietin.PloS one · 2015Article
- Multifarious determinants of cytokine receptor signaling specificity.Advances in immunology · 2014Review
- Clinical pharmacokinetics and pharmacodynamics of erythropoiesis-stimulating agents.Clinical pharmacokinetics · 2013Review
- The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011Review
- Topological transformation of liposomes by a membrane-affecting domain of recombinant human erythropoietin.Journal of liposome research · 2010Article
- Erythropoietin blockade inhibits the induction of tumor angiogenesis and progression.PloS one · 2007Article
- Design of homogeneous, monopegylated erythropoietin analogs with preserved in vitro bioactivity.Experimental hematology · 2006Article
- Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Structural and functional hot spots in cytokine receptors.International journal of hematology · 2001Review
- Dominant action of mutated erythropoietin receptors on differentiation in vitro and erythroleukemia development in vivo.Oncogene · 2000Article
- Activation of erythropoietin receptor in the absence of hormone by a peptide that binds to a domain different from the hormone binding site.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Macromolecular docking of a three-body system: the recognition of human growth hormone by its receptor.Protein science : a publication of the Protein Society · 1999Article
- Recombinant herpes simplex virus type 1 engineered for targeted binding to erythropoietin receptor-bearing cells.Journal of virology · 1998Article
- Human thrombopoietin structure-function relationships: identification of functionally important residues.The Biochemical journal · 1998Article
- Characterization of the receptor binding determinants of granulocyte colony stimulating factor.Protein science : a publication of the Protein Society · 1997Article
- Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have probed the interaction of human erythropoietin (EPO) with its receptor (EPO-R) by analyzing a panel of 17 EPO mutants in a variety of in vitro assays. Mutant proteins were expressed in 293s cells and quantified by using an N-terminal epitope tag in conjunction with a surface plasmon resonance assay. Receptor binding was studied using both a soluble form of the EPO-R extracellular domain in an ELISA-format binding competition assay and full-length EPO-R in transfected BaF3 cells. Proliferative activity of the mutants was also determined in the BaF3-derived cell line and was correlated with the results from binding assays. Based on the results of these assays, we identified two distinct receptor binding sites on the EPO molecule. We propose that one site, containing residues Arg-150 and Lys-152, binds initially to EPO receptor on the cell surface. A second site, containing Arg-103 and Ser-104 (and possibly Arg-14), is involved in binding a second EPO-R at the cell surface, thus forming a homodimeric receptor complex. Furthermore, we demonstrate that one EPO mutant (R103A), which has previously been shown to lack proliferative function, is in fact an EPO antagonist. Taken together, these data support a sequential dimerization mechanism of EPO-R activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.