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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Protein inhibitor of activated STAT, 4

PIASy, PIASgamma
Top mentioned proteins: Smt3, Ubiquitin, DAPI, CAN, SUMO-2
Papers on PIASy
Protein Inhibitor of Activated STAT3 Regulates Migration, Invasion, and Activation of Fibroblast-like Synoviocytes in Rheumatoid Arthritis.
Xu et al., Guangzhou, China. In J Immunol, Feb 2016
Protein inhibitor of activated STAT (PIAS), whose family members include PIAS1, PIAS2 (PIASx), PIAS3, and PIAS4 (PIASy), play important roles in regulating various cellular events, such as cell survival, migration, and signal transduction in many cell types.
SUMOylation and Ubiquitylation Circuitry Controls Pregnane X Receptor Biology in Hepatocytes.
Staudinger et al., United States. In Drug Metab Dispos, Sep 2015
The SUMO-E3 ligase enzymes protein inhibitor of activated signal transducer and activator of transcription-1 (STAT1) STAT-1 (PIAS1) and protein inhibitor of activated STAT Y (PIASy) drive high levels of PXR SUMOylation.
Implication of SUMO E3 ligases in nucleotide excision repair.
Iijima et al., Nagoya, Japan. In Cytotechnology, Aug 2015
In the present study, we performed RNAi knockdown of SUMO E3 ligases and found that, in addition to PIASy, the polycomb protein Pc2 affected the repair of cyclobutane pyrimidine dimers.
HIF-1α SUMOylation affects the stability and transcriptional activity of HIF-1α in human lens epithelial cells.
Yan et al., Shenyang, China. In Graefes Arch Clin Exp Ophthalmol, Aug 2015
In the present study, we examined SUMO and SUMO E3 (Cbx4 and PIASy) expression induced by high glucose, and investigated SUMO or SUMO E3 overexpression that enhanced HIF-1α SUMOylation in HLECs.
The E3 ubiquitin ligase TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2.
Spencer et al., Los Angeles, United States. In Hum Mol Genet, Jun 2015
This satellite cell senescence is due to accumulation of the SUMO ligase PIASy, a substrate of TRIM32.
An LRP16-containing preassembly complex contributes to NF-κB activation induced by DNA double-strand breaks.
Han et al., Beijing, China. In Nucleic Acids Res, May 2015
The concomitant SUMOylation and phosphorylation of IKKγ by PIASy and ATM, respectively, is a key event in this mechanism.
SUMOylation regulates polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis.
Azuma et al., Lawrence, United States. In J Biol Chem, Mar 2015
PICH SUMOylation is highly dependent on protein inhibitor of activated STAT, PIASy, consistent with other mitotic chromosomal SUMO substrates.
A dysregulated acetyl/SUMO switch of FXR promotes hepatic inflammation in obesity.
Kemper et al., Urbana, United States. In Embo J, Feb 2015
Mechanistically, acetylation of FXR blocked its interaction with the SUMO ligase PIASy and inhibited SUMO2 modification at K277, resulting in activation of inflammatory genes.
SUMO Proteins are not Involved in TGF-β1-induced, Smad3/4-mediated Germline α Transcription, but PIASy Suppresses it in CH12F3-2A B Cells.
Park et al., Taejŏn, South Korea. In Immune Netw, 2014
Next, we tested the effect of the E3 ligase PIASy on TGF-β1-induced, Smad3/4-mediated GLα promoter activity.
SUMOylation of Psmd1 controls Adrm1 interaction with the proteasome.
Dasso et al., Bethesda, United States. In Cell Rep, 2014
Psmd1 becomes SUMOylated through the action of the SUMO E3 enzyme PIASy.
PIAS4 represses vitamin D receptor-mediated signaling and acts as an E3-SUMO ligase towards vitamin D receptor.
Thompson et al., Coleraine, United Kingdom. In J Steroid Biochem Mol Biol, 2012
PIAS4 and the process of SUMOylation are important modulators of Vitamin D receptor-mediated signaling
SYT-SSX1 (synovial sarcoma translocated) regulates PIASy ligase activity to cause overexpression of NCOA3 protein.
Huang et al., Los Angeles, United States. In J Biol Chem, 2011
The increase of NCOA3 is essential for SYT-SSX1-mediated synovial sarcoma formation. SYT-SSX1 does so by increasing the sumoylation of NCOA3 through interaction with a SUMO E3 ligase, PIASy, as well as the sumoylation of NEMO.
Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization.
Insel et al., San Diego, United States. In J Biol Chem, 2011
Cav-3 is SUMOylated in a manner that is enhanced by the SUMO E3 ligase PIASy; Cav-3 SUMOylation in the mechanisms for beta(2)AR but not beta(1)AR desensitization
PIASy inhibits virus-induced and interferon-stimulated transcription through distinct mechanisms.
Ozato et al., Tokyo, Japan. In J Biol Chem, 2011
PIASy negatively regulates both IFN transcription and IFN-stimulated gene expression through multiple mechanisms utilizing the function of different domains.
PIASy stimulates HIF1α SUMOylation and negatively regulates HIF1α activity in response to hypoxia.
Cheng et al., Shanghai, China. In Oncogene, 2010
Studies define an important role of PIASy in hypoxia signaling through promoting HIF1alpha SUMOylation.
Novel initiation genes in squamous cell carcinomagenesis: a role for substrate-specific ubiquitylation in the control of cell survival.
Kulesz-Martin et al., Portland, United States. In Mol Carcinog, 2007
Trim32 binds and ubiquitylates Piasy, controlling its stability and accumulation.
C-terminal modifications regulate MDM2 dissociation and nuclear export of p53.
Vousden et al., Glasgow, United Kingdom. In Nat Cell Biol, 2007
Monoubiquitination can directly promote further modifications of p53 with ubiquitin-like proteins and MDM2 promotes the interaction of the SUMO E3 ligase PIASy with p53, enhancing both sumoylation and nuclear export.
SUMO is growing senescent.
Dejean et al., Paris, France. In Cell Cycle, 2007
We have shown recently that the E3 SUMO ligase PIASy actively contributes to execution of the senescence program, thus, providing the first evidence for a direct role of SUMO modification in this process.
PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress.
Miyamoto et al., Madison, United States. In Nat Cell Biol, 2006
PIASy is the first SUMO ligase for NEMO whose substrate specificity seems to be controlled by IKK interaction, subcellular targeting and oxidative stress conditions.
Synergy of glucose and growth hormone signalling in islet cells through ICA512 and STAT5.
Solimena et al., Dresden, Germany. In Nat Cell Biol, 2006
Sumoylation of ICA512 by the E3 SUMO ligase PIASy, in turn, may reverse this process by decreasing the binding of ICA512 to STAT5.
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