ArticleMolecular and cellular biology1996
Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 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
68 citing papers in PubMed, 264 citations in OpenAlex.
- Dissecting Selectivity Determinants of Small-Molecule Inhibitors of SH2 Domains Via Fluorescence Polarization Assays.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Cytokine receptor splice variants in hematologic diseases.Cytokine · 2020Review
- Transcriptional Regulation of Emergency Granulopoiesis in Leukemia.Frontiers in immunology · 2018Review
- Review
- Erythropoietin Does Not Enhance Skeletal Muscle Protein Synthesis Following Exercise in Young and Older Adults.Frontiers in physiology · 2016Article
- Effect of alpha lipoic acid on retinal ganglion cell survival in an optic nerve crush model.Molecular vision · 2016Article
- Nanomolar inhibitors of the transcription factor STAT5b with high selectivity over STAT5a.Angewandte Chemie (International ed. in English) · 2015Article
- Tricyclic covalent inhibitors selectively target Jak3 through an active site thiol.The Journal of biological chemistry · 2015Article
- Erythropoietin action in stress response, tissue maintenance and metabolism.International journal of molecular sciences · 2014Review
- EPO-receptor is present in mouse C2C12 and human primary skeletal muscle cells but EPO does not influence myogenesis.Physiological reports · 2014Article
- The role of glucocorticoid receptor (GR) polymorphisms in human erythropoiesis.American journal of blood research · 2014Article
- Erythropoietin, a novel versatile player regulating energy metabolism beyond the erythroid system.International journal of biological sciences · 2014Review
- Enhancement of ventricular-subventricular zone-derived neurogenesis and oligodendrogenesis by erythropoietin and its derivatives.Frontiers in cellular neuroscience · 2013Review
- The role and regulation of erythropoietin (EPO) and its receptor in skeletal muscle: how much do we really know?Frontiers in physiology · 2013Article
- Novel multiplexed assay for identifying SH2 domain antagonists of STAT family proteins.PloS one · 2013Article
- STAT5 triggers BCR-ABL1 mutation by mediating ROS production in chronic myeloid leukaemia.Oncotarget · 2012Article
- Article
- Differential proteomic analysis of human erythroblasts undergoing apoptosis induced by epo-withdrawal.PloS one · 2012Article
- Chromatin condensation via the condensin II complex is required for peripheral T-cell quiescence.The EMBO journal · 2011Article
- Erythropoietin protects against diabetes through direct effects on pancreatic beta cells.The Journal of experimental medicine · 2010Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The cytoplasmic domain of the erythropoietin receptor (EpoR) contains a membrane-distal region that is dispensable for mitogenesis but is required for the recruitment and tyrosine phosphorylation of a variety of signaling proteins. The membrane-proximal region of 96 amino acids is necessary and sufficient for mitogenesis as well as Jak2 activation, induction of c-fos, c-myc, cis, the T-cell receptor gamma locus (TCR-gamma), and c-pim-1. The studies presented here demonstrate that this region is also necessary and sufficient for the activation of Stat5A and Stat5B. The membrane-proximal domain contains a single tyrosine, Y-343, which when mutated eliminates the ability of the receptor to couple Epo binding to the activation of Stat5. Furthermore, peptide competitions demonstrate that this site, when phosphorylated, can disrupt Stat5 DNA binding activity, consistent with a role of Y-343 as a site of recruitment to the receptor. Cells expressing the truncated, Y343F mutant (a mutant with a Y-to-F alteration at position 343) proliferate in response to Epo in a manner comparable to that of the controls. However, in these cells, Epo stimulation does not induce the appearance of transcripts for cis, TCR-gamma, or c-fos, suggesting a role for Stat5 in their regulation.
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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.