ArticleProceedings of the National Academy of Sciences of the United States of America1997
Stat5 is a physiological substrate of the insulin receptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 123 citations in OpenAlex.
- Insulin and GH signaling in human skeletal muscle in vivo following exogenous GH exposure: impact of an oral glucose load.PloS one · 2011Trial
- Mammary gland development and function in maternal obesity and gestational diabetes.Current opinion in physiology · 2026Article
- Disease-associated mutations in the STAT5B SH2 domain reprogram hepatic cholesterol and lipid metabolism.Endocrinology · 2026Article
- Disease-associated mutations in the STAT5B SH2 domain reprogram hepatic cholesterol and lipid metabolism.bioRxiv : the preprint server for biology · 2025Article
- Effects of heterologous kinase domains on growth factor receptor specificity.Cellular signalling · 2024Article
- Genetic Modulation of the GLUT1 Transporter Expression-Potential Relevance in Complex Diseases.Biology · 2022Article
- An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation.Nature communications · 2022Article
- Programmed Death-Ligand 1 (PD-L1) Expression Is Induced by Insulin in Pancreatic Ductal Adenocarcinoma Cells Pointing to Its Role in Immune Checkpoint Control.Medical sciences (Basel, Switzerland) · 2021Article
- Regulation of the JAK2-STAT5 Pathway by Signaling Molecules in the Mammary Gland.Frontiers in cell and developmental biology · 2020Review
- Skeletal muscle mitochondrial function and exercise capacity are not impaired in mice with knockout of STAT3.Journal of applied physiology (Bethesda, Md. : 1985) · 2019Article
- IGF-1-induced MMP-11 expression promotes the proliferation and invasion of gastric cancer cells through the JAK1/STAT3 signaling pathway.Oncology letters · 2018Article
- Mammalian target of rapamycin complex 2 regulates muscle glucose uptake during exercise in mice.The Journal of physiology · 2017Article
- PI3K signaling and Stat92E converge to modulate glial responsiveness to axonal injury.PLoS biology · 2014Article
- Hepatic oxidative stress promotes insulin-STAT-5 signaling and obesity by inactivating protein tyrosine phosphatase N2.Cell metabolism · 2014Article
- Inputs and outputs of insulin receptor.Protein & cell · 2014Review
- Insulin and IGFs in obesity-related breast cancer.Journal of mammary gland biology and neoplasia · 2013Review
- JAK-STAT signaling and myocardial glucose metabolism.JAK-STAT · 2013Review
- Novel roles for insulin receptor (IR) in adipocytes and skeletal muscle cells via new and unexpected substrates.Cellular and molecular life sciences : CMLS · 2013Review
- Molecular basis of signaling specificity of insulin and IGF receptors: neglected corners and recent advances.Frontiers in endocrinology · 2012Article
- Signaling by vitamin A and retinol-binding protein in regulation of insulin responses and lipid homeostasis.Biochimica et biophysica acta · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Using the cytoplasmic domain of the insulin receptor (IR) in a yeast two-hybrid screen, we identified a cDNA clone encoding the C-terminal 308 amino acids of human Stat5b (Stat5b-Ct). Stat5b-Ct is tyrosine phosphorylated by purified IR kinase domain in vitro. Insulin stimulates tyrosine phosphorylation of overexpressed Stat5b-Ct and endogenous Stat5 in cells overexpressing IR. Stat5 may be a direct target of the IR and, as a member of the Stat family of transcription factors, may play a role in the regulation of gene transcription by insulin. In support of this hypothesis, perfusion of mouse liver with insulin promotes rapid tyrosine phosphorylation of Stat5 and activation of Stat5 DNA binding. Moreover, refeeding of fasted mice leads to rapid tyrosine phosphorylation and stimulation of enhanced DNA-binding activity of Stat5 extracted from liver, skeletal muscle, and adipose tissues. Taken together, our data strongly suggest that IR interacts with and phosphorylates Stat5 in vitro and in tissues physiologically sensitive to insulin.
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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.