ArticleMolecular and cellular biology1995
Differentiation-regulated serine phosphorylation of STAT1 promotes GAF activation in macrophages.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 101 citations in OpenAlex.
- Article
- Review
- Cold Storage Followed by Transplantation Induces Interferon-Gamma and STAT-1 in Kidney Grafts.International journal of molecular sciences · 2023Article
- Responses to Cytokines and Interferons that Depend upon JAKs and STATs.Cold Spring Harbor perspectives in biology · 2018Review
- CDK8 as the STAT1 serine 727 kinase?JAK-STAT · 2013Article
- Smurf1 protein negatively regulates interferon-γ signaling through promoting STAT1 protein ubiquitination and degradation.The Journal of biological chemistry · 2012Article
- Activation of the JAK/STAT-1 signaling pathway by IFN-gamma can down-regulate functional expression of the MHC class I-related neonatal Fc receptor for IgG.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- Signalling events involved in interferon-gamma-inducible macrophage nitric oxide generation.Immunology · 2003Article
- IL-6 mediated activation of STAT3 bypasses Janus kinases in terminally differentiated B lineage cells.Oncogene · 2002Article
- Biphasic regulation of extracellular-signal-regulated protein kinase by leptin in macrophages: role in regulating STAT3 Ser727 phosphorylation and DNA binding.The Biochemical journal · 2002Article
- Stat1-vitamin D receptor interactions antagonize 1,25-dihydroxyvitamin D transcriptional activity and enhance stat1-mediated transcription.Molecular and cellular biology · 2002Article
- Article
- The role of STAT proteins in growth hormone signaling.Oncogene · 2000Review
- Serine phosphorylation of STATs.Oncogene · 2000Review
- Regulation of CD26/DPPIV gene expression by interferons and retinoic acid in tumor B cells.Oncogene · 2000Article
- Inhibition of protein phosphatase 2A induces serine/threonine phosphorylation, subcellular redistribution, and functional inhibition of STAT3.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Rapid inhibition of interleukin-6 signaling and Stat3 activation mediated by mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Stat1 combines signals derived from IFN-gamma and LPS receptors during macrophage activation.The EMBO journal · 1998Article
- Group B streptococci persist inside macrophages.Immunology · 1998Article
- Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription.Molecular and cellular biology · 1997Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gamma interferon (IFN-gamma), a macrophage-activating cytokine, modulates gene expression through the activity of a transcription factor designated IFN-gamma activation factor (GAF). GAF is formed after phosphorylation on tyrosine and dimerization of the 91-kDa protein STAT1. We have recently reported that differentiation of the promonocytic cell line U937 into monocytes increases the amount of cellular GAF after IFN-gamma treatment and at the same time increases the phosphorylation of STAT1. Here we show that activation of the JAK family kinases, which are instrumental in mediating STAT1 phosphorylation on tyrosine, did not increase upon monocytic U937 differentiation. Consistent with this finding, levels of STAT1 tyrosine phosphorylation were virtually identical in promonocytic and monocytic U937 cells. Analysis of STAT1 phosphoamino acids and mapping of phosphopeptides showed an IFN-gamma-dependent increase in Ser phosphorylation in differentiated cells. Analyses of STAT1 isoforms by two-dimensional gel electrophoresis demonstrated a differentiation-induced shift toward more acidic isoforms. All isoforms were equally sensitive to subsequent tyrosine phosphorylation, as indicated by a sodium dodecyl sulfate-polyacrylamide gel electrophoresis mobility shift typical for tyrosine-phosphorylated STAT1. Consistent with the importance of Ser phosphorylation for high-affinity binding to the IFN-gamma activation site sequence, phosphatase 2A treatment strongly reduced the formation of IFN-gamma activation site-GAF complexes in an electrophoretic mobility shift assay. Our data indicate that the activity of GAF is modulated by STAT1 serine kinases/phosphatases and suggest that this mechanism is employed in the developmental control of macrophage responsiveness to IFN-gamma.
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