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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 01 Mar 2015.

Signal transducer and activator of transcription 2, 113kDa

STAT2
The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. In response to interferon (IFN), this protein forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with this protein, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: STAT1, STAT3, CAN, IFN-gamma, Janus kinase
Papers on STAT2
Decreased STAT3 in human idiopathic fetal growth restriction contributes to trophoblast dysfunction.
New
Murthi et al., Australia. In Reproduction, 23 Mar 2015
Expression profiling of FGR-affected placentae revealed mRNA levels of STAT3, STAT2 and STAT5B decreased by 69%, 52% and 50%, respectively, compared with gestational-age matched controls.
Set7 Facilitates Hepatitis C Virus Replication via Enzymatic Activity-Dependent Attenuation of the IFN-Related Pathway.
New
Zhu et al., Wuhan, China. In J Immunol, 13 Mar 2015
Further investigation suggested that Set7 suppressed the endogenous IFN expression by reducing the nuclear translocation of IFN regulatory factor 3/7 and the p65 subunit of NF-κB and reduced IFN-induced dsRNA-activated protein kinase and 2',5'-oligoadenylate synthetase via attenuation of the phosphorylation of STAT1 and STAT2.
Dengue Virus Control of Type I IFN Responses: A History of Manipulation and Control.
New
Urcuqui-Inchima et al., Medellín, Colombia. In J Interferon Cytokine Res, 28 Feb 2015
In addition, the viral proteins, NS2A, NS4A, NS4B, and NS5, can inhibit IFN-I signaling by blocking the phosphorylation of the STAT1 and STAT2 molecules.
Disruption of Type I Interferon Signaling by NSs Protein of Severe Fever with Thrombocytopenia Syndrome Virus via Hijacking STAT2 and STAT1 into Inclusion Bodies.
New
Wang et al., Wuhan, China. In J Virol, 28 Feb 2015
Furthermore, co-immunoprecipitation (Co-IP) and pull-down assays indicated that NSs interacts with the cellular signal transducer and activator of transcription 2 (STAT2) and the DNA-binding domain of STAT2 may contribute to the NSs-STAT2 interaction.
Targeting interferon response genes sensitizes aromatase inhibitor resistant breast cancer cells to estrogen-induced cell death.
New
Lewis-Wambi et al., In Breast Cancer Res, 15 Feb 2015
In the present study, we assessed the functional role of IFITM1 and PLSCR1; two well-known interferon response genes in AI resistance.MethodsReal-time PCR and Western blot analyses were used to assess mRNA and protein levels of IFITM1, PLSCR1, STAT1, STAT2, and IRF-7 in AI-resistant MCF-7:5C breast cancer cells and AI-sensitive MCF-7 and T47D cells.
Toward a new STATe: the role of STATs in mitochondrial function.
Review
New
Larner et al., Richmond, United States. In Semin Immunol, Feb 2014
Recently, other members of the STAT family (STAT1, STAT2, STAT5, and STAT6) have also been shown to be present in the mitochondria.
STAT2 signaling and dengue virus infection.
Review
García-Sastre et al., Seattle, United States. In Jakstat, 2014
This review describes strategies that DENV uses to evade the type I interferon response and focuses on how data gained from the study of DENV NS5-mediated STAT2 degradation may be used to create immunocompetent DENV mouse models and design anti-DENV therapeutics.
STAT2 and IRF9: Beyond ISGF3.
Review
Grandvaux et al., Montréal, Canada. In Jakstat, 2013
Among STATs, STAT2 is classically known to dimerize with STAT1 and together with IRF9 forms the ISGF3 transcription factor complex that has long been considered a hallmark of activation by type I and type III interferons.
STATs get their move on.
Review
Reich, Stony Brook, United States. In Jakstat, 2013
Following STAT2 tyrosine phosphorylation, it can form dimers with STAT1 to affect nuclear import as the trimeric complex (ISGF3).
STAT2 phosphorylation and signaling.
Review
Gamero et al., Philadelphia, United States. In Jakstat, 2013
Evidence of additional STAT2 phosphorylation sites has emerged as well as novel roles for STAT2 separate from the classical ISGF3-signaling.
A variant upstream of IFNL3 (IL28B) creating a new interferon gene IFNL4 is associated with impaired clearance of hepatitis C virus.
Impact
O'Brien et al., Bethesda, United States. In Nat Genet, 2013
Transient overexpression of IFNL4 in a hepatoma cell line induced STAT1 and STAT2 phosphorylation and the expression of interferon-stimulated genes.
A haplotype at STAT2 Introgressed from neanderthals and serves as a candidate of positive selection in Papua New Guinea.
GeneRIF
Hammer et al., Tucson, United States. In Am J Hum Genet, 2012
A haplotype at STAT2 introgressed from neanderthals serves as a candidate of positive selection in Papua New Guinea.
HSV-2 inhibits type-I interferon signaling via multiple complementary and compensatory STAT2-associated mechanisms.
GeneRIF
Foster et al., New Orleans, United States. In Virus Res, 2012
These results indicate the importance that herpes simplex virus 2 has assigned to STAT2, investing significant genomic currency throughout its replicative lifecycle for continuous targeted destruction and inhibition of this protein.
Mice deficient in STAT1 but not STAT2 or IRF9 develop a lethal CD4+ T-cell-mediated disease following infection with lymphocytic choriomeningitis virus.
GeneRIF
Campbell et al., Sydney, Australia. In J Virol, 2012
STAT1, not STAT2 or IRF9, prevent the emergence of a lethal antiviral CD4(+) T-cell response after lymphocytic choriomeningitis virus infection.
The JAK-STAT pathway at twenty.
Review
Impact
Darnell et al., Cleveland, United States. In Immunity, 2012
We look back on the discoveries that the tyrosine kinases TYK2 and JAK1 and the transcription factors STAT1, STAT2, and IRF9 are required for the cellular response to type I interferons.
Gene expression profile reveals that STAT2 is involved in the immunosuppressive function of human bone marrow-derived mesenchymal stem cells.
GeneRIF
Song et al., Inch'ŏn, South Korea. In Gene, 2012
STAT2 is functionally involved in the immunosuppressive activity of hcMSCs as a novel regulator under inflammatory conditions.
The transcription factor STAT2 enhances proteasomal degradation of RCAN1 through the ubiquitin E3 ligase FBW7.
GeneRIF
Chung et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2012
Co-immunoprecipitation/immunoblot analyses showed that STAT2 enhanced RCAN1 ubiquitination through the ubiquitin E3 ligase FBW7..
NLRX1 protein attenuates inflammatory responses to infection by interfering with the RIG-I-MAVS and TRAF6-NF-κB signaling pathways.
Impact
Ting et al., Chapel Hill, United States. In Immunity, 2011
We showed that Nlrx1(-/-) mice exhibited increased expression of antiviral signaling molecules IFN-β, STAT2, OAS1, and IL-6 after influenza virus infection.
Nonconventional initiation complex assembly by STAT and NF-kappaB transcription factors regulates nitric oxide synthase expression.
Impact
Decker et al., Vienna, Austria. In Immunity, 2010
Here we showed sequential and cooperative contributions of the transcription factors ISGF3 (a complex containing STAT1, STAT2, and IRF9 subunits) and NF-kappaB to the transcriptional induction of the Nos2 gene in macrophages infected with the intracellular bacterial pathogen Listeria monocytogenes.
Acetylation-dependent signal transduction for type I interferon receptor.
Impact
Chin et al., Providence, United States. In Cell, 2007
IRF9 interacts with the acetyl-Lys399 motif by means of its IRF homology2 (IH2) domain, leading to formation of the ISGF3 complex that includes IRF9, STAT1, and STAT2.
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