ArticleMolecular and cellular biology1994
Growth hormone and erythropoietin differentially activate DNA-binding proteins by tyrosine phosphorylation.
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 20 papers.
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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
20 citing papers in PubMed, 90 citations in OpenAlex.
- 2022 Cannon lecture: an ode to signal transduction: how the growth hormone pathway revealed insight into height, malignancy, and obesity.American journal of physiology. Endocrinology and metabolism · 2023Review
- Modeling the Hematopoietic Landscape.Frontiers in cell and developmental biology · 2019Review
- The ebola virus interferon antagonist VP24 directly binds STAT1 and has a novel, pyramidal fold.PLoS pathogens · 2012Article
- Phagocytosis mediated by Yersinia invasin induces collagenase-1 expression in rabbit synovial fibroblasts through a proinflammatory cascade.Journal of cell science · 2001Article
- A plasma kallikrein-dependent plasminogen cascade required for adipocyte differentiation.Nature cell biology · 2001Article
- Stromelysin-1 regulates adipogenesis during mammary gland involution.The Journal of cell biology · 2001Article
- Stat1 associates with c-kit and is activated in response to stem cell factor.The Biochemical journal · 1997Article
- Identification of tyrosine residues within the intracellular domain of the erythropoietin receptor crucial for STAT5 activation.The EMBO journal · 1996Article
- The regulation of protein transport to the nucleus by phosphorylation.The Biochemical journal · 1995Review
- Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases by interleukins 2 and 15.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- STAT protein complexes activated by interferon-gamma and gp130 signaling molecules differ in their sequence preferences and transcriptional induction properties.Nucleic acids research · 1995Article
- Signaling through the interleukin 2 receptor beta chain activates a STAT-5-like DNA-binding activity.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Interleukin 12 induces tyrosine phosphorylation and activation of STAT4 in human lymphocytes.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- STAT3 activation by cytokines utilizing gp130 and related transducers involves a secondary modification requiring an H7-sensitive kinase.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Thrombopoietin activates a STAT5-like factor in hematopoietic cells.The EMBO journal · 1995Article
- Cloning of murine Stat6 and human Stat6, Stat proteins that are tyrosine phosphorylated in responses to IL-4 and IL-3 but are not required for mitogenesis.Molecular and cellular biology · 1995Article
- Prolactin, growth hormone, erythropoietin and granulocyte-macrophage colony stimulating factor induce MGF-Stat5 DNA binding activity.The EMBO journal · 1995Article
- Growth hormone rapidly activates rat serine protease inhibitor 2.1 gene transcription and induces a DNA-binding activity distinct from those of Stat1, -3, and -4.Molecular and cellular biology · 1995Article
- Signal transduction and activation of gene transcription by interferons.Gene expression · 1995Review
- Activation of JAK kinases and STAT proteins by interleukin-2 and interferon alpha, but not the T cell antigen receptor, in human T lymphocytes.The EMBO journal · 1994Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
Binding of growth hormone (GH) and erythropoietin (EPO) to their respective receptors results in receptor clustering and activation of tyrosine kinases that initiate a cascade of events resulting not only in the rapid tyrosine phosphorylation of several proteins but also in the induction of early-response genes. In this report, we show that GH and EPO induce the tyrosine phosphorylation of cellular proteins with molecular masses of 93 kDa and of 91 and 84 kDa, respectively, and that these proteins form DNA-binding complexes which recognize an enhancer that has features in common with several rapidly induced genes such as c-fos. Assembly of the protein complexes required tyrosine phosphorylation, which occurred within minutes after addition of ligand. The activated complexes translocated from the cytoplasm to the nucleus. The protein activated by GH is antigenically similar to p91, a protein common to several transcription complexes that are activated by interferons and other cytokines. In contrast, the proteins activated by EPO are distinct from p91. These findings establish the outlines for a cytokine-induced intracellular signaling pathway, which begins with ligand-induced receptor clustering that activates one or more tyrosine kinases. These data are the first to demonstrate that GH- and EPO-activated tyrosine-phosphorylated proteins can specifically recognize a well-defined enhancer and therefore provide a mechanism for rapidly transducing signals from the membrane to the nucleus.
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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.