ArticleThe EMBO journal1996
Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
43 citing papers in PubMed, 203 citations in OpenAlex.
- Article
- Cytokine receptor splice variants in hematologic diseases.Cytokine · 2020Review
- Cytokine-mediated communication: a quantitative appraisal of immune complexity.Nature reviews. Immunology · 2019Review
- The role of suppressors of cytokine signalling in human neoplasms.Molecular biology international · 2014Review
- Biology and significance of the JAK/STAT signalling pathways.Growth factors (Chur, Switzerland) · 2012Review
- The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011Review
- Division of labor by dual feedback regulators controls JAK2/STAT5 signaling over broad ligand range.Molecular systems biology · 2011Article
- An extra high dose of erythropoietin fails to support the proliferation of erythropoietin dependent cell lines.Cytotechnology · 2011Article
- Advances in understanding the pathogenesis of primary familial and congenital polycythaemia.British journal of haematology · 2010Review
- STAT5 activation is critical for the transformation mediated by myeloproliferative disorder-associated JAK2 V617F mutant.The Journal of biological chemistry · 2010Article
- Role of the JNK/c-Jun/AP-1 signaling pathway in galectin-1-induced T-cell death.Cell death & disease · 2010Article
- Translational isoforms of FOG1 regulate GATA1-interacting complexes.The Journal of biological chemistry · 2009Article
- Inactivation of G-protein-coupled receptor 48 (Gpr48/Lgr4) impairs definitive erythropoiesis at midgestation through down-regulation of the ATF4 signaling pathway.The Journal of biological chemistry · 2008Article
- Review
- Article
- Signal transducers and activators of transcription 5 contributes to erythropoietin-mediated neuroprotection against hippocampal neuronal death after transient global cerebral ischemia.Neurobiology of disease · 2007Article
- Article
- Signals for stress erythropoiesis are integrated via an erythropoietin receptor-phosphotyrosine-343-Stat5 axis.The Journal of clinical investigation · 2006Article
- Phosphatidylinositol 3-kinase/Akt induced by erythropoietin renders the erythroid differentiation factor GATA-1 competent for TIMP-1 gene transactivation.Molecular and cellular biology · 2005Article
- Cytokine signals through STAT3 promote expression of granulocyte secondary granule proteins in 32D cells.Experimental hematology · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FDCP-1 cells are hematopoietic progenitor cells which require interleukin-3 for survival and proliferation. FDCP-1 cells stably transfected with the murine erythropoietin receptor cDNA survive and proliferate in the presence of erythropoietin. Erythropoietin induces the activation of the short forms (80 kDa) of STAT5 in the cells. Erythropoietin-induced activation of STAT5 was strongly reduced in cells expressing mutated variants of the erythropoietin receptors in which tyrosine residues in their intracellular domain have been eliminated. We determined that the erythropoietin receptor tyrosine residues 343 and 401 are independently necessary for STAT5 activation. The amino acid sequences surrounding these two tyrosine residues are very similar. Peptides comprising either phosphorylated Tyr343 or phosphorylated Tyr401, but not their unphosphorylated counterparts, inhibited the STAT5 activation. We propose that these two tyrosine residues of the erythropoietin receptor constitute docking sites for the STAT5 SH2 domain. The growth stimulus mediated by erythropoietin was decreased in cells expressing erythropoietin receptors lacking both Tyr343 and Tyr401. This suggests that STAT5 activation could be involved in the growth control of FDCP-1 cells.
Indexed as
Identifiers
8665851PMC450175W1900781903What OpenQuestion holds
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.