ArticleThe Journal of biological chemistry2013
Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 31 citations in OpenAlex.
- Sarbecoviruses Suppress Innate Immunity by Recruiting PPM1A to Modulate STAT2 and ORF9b Phosphorylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- SENP5 enhances antiviral innate immunity by promoting AURKA-dependent STAT2 phosphorylation.Cell communication and signaling : CCS · 2026Article
- Transcriptional control of interferon-stimulated genes.The Journal of biological chemistry · 2024Review
- Comprehensive literature review of monkeypox.Emerging microbes & infections · 2022Review
- Exposing the Two Contrasting Faces of STAT2 in Inflammation.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2022Review
- Human Disease Phenotypes Associated with Loss and Gain of Function Mutations in STAT2: Viral Susceptibility and Type I Interferonopathy.Journal of clinical immunology · 2021Review
- Review
- Stat2 stability regulation: an intersection between immunity and carcinogenesis.Experimental & molecular medicine · 2020Review
- FBXW7-mediated stability regulation of signal transducer and activator of transcription 2 in melanoma formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Interferon signaling in cancer. Non-canonical pathways and control of intracellular immune checkpoints.Seminars in immunology · 2019Review
- Differential Regulation of Type I and Type III Interferon Signaling.International journal of molecular sciences · 2019Review
- Fine-Tuning of Type I Interferon Response by STAT3.Frontiers in immunology · 2019Review
- Bclaf1 critically regulates the type I interferon response and is degraded by alphaherpesvirus US3.PLoS pathogens · 2019Article
- Responses to Cytokines and Interferons that Depend upon JAKs and STATs.Cold Spring Harbor perspectives in biology · 2018Review
- Transcriptional Regulation of Antiviral Interferon-Stimulated Genes.Trends in microbiology · 2017Review
- Negative regulation of type I IFN signaling by phosphorylation of STAT2 on T387.The EMBO journal · 2017Article
- Interplay between Janus Kinase/Signal Transducer and Activator of Transcription Signaling Activated by Type I Interferons and Viral Antagonism.Frontiers in immunology · 2017Review
- Phosphorylation of STAT2 on serine-734 negatively regulates the IFN-α-induced antiviral response.Journal of cell science · 2016Article
- The Tumor Suppressive Effects of HPP1 Are Mediated Through JAK-STAT-Interferon Signaling Pathways.DNA and cell biology · 2015Article
- Protein tyrosine phosphatases as wardens of STAT signaling.JAK-STAT · 2014Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
STAT2 is a positive modulator of the transcriptional response to type I interferons (IFNs). STAT2 acquires transcriptional function by becoming tyrosine phosphorylated and imported to the nucleus following type I IFN receptor activation. Although most STAT proteins become dually phosphorylated on specific tyrosine and serine residues to acquire full transcriptional activity, no serine phosphorylation site in STAT2 has been reported. To find novel phosphorylation sites, mass spectrometry of immunoprecipitated STAT2 was used to identify several phosphorylated residues. Of these, substitution of serine 287 with alanine (S287A) generated a gain-of-function mutant that enhanced the biological effects of IFN-α. S287A-STAT2 increased cell growth inhibition, prolonged protection against vesicular stomatitis virus infection and enhanced transcriptional responses following exposure of cells to IFN-α. In contrast, a phosphomimetic STAT2 mutant (S287D) produced a loss-of-function protein that weakly activated IFN-induced ISGs. Our mechanistic studies suggest that S287A-STAT2 likely mediates its gain-of-function effects by prolonging STAT2/STAT1 dimer activation and retaining it in transcriptionally active complexes with chromatin. Altogether, we have uncovered that in response to type I IFN, STAT2 is serine phosphorylated in the coiled-coil domain that when phosphorylated can negatively regulate the biological activities of type I IFNs.
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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.