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Findings indicate that protein inhibitor of activated STAT 4 (PIAS4) mediated SIRT1 (show SIRT1 Proteins) repression in response to nutrient surplus contributes to the pathogenesis of Nonalcoholic Steatohepatitis (NASH (show SAMSN1 Proteins)).
new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFbeta (show TGFB1 Proteins) signaling pathway through the site-specific ubiquitination of PIAS4.
PKA-induced SREBP1c (show SREBF1 Proteins) sumoylation by PIASy.
the SUMO E3 ligase (show PIAS1 Proteins) PIASy (also known as PIAS4) was induced by hypoxia and prevented Sp1 (show SP1 Proteins) from binding to the SIRT1 (show SIRT1 Proteins) promoter.
Piasy represses the synergistic activation of PITX2 (show PITX2 Proteins) with interacting co-factors and Piasy represses Pias1 (show PIAS1 Proteins) activation of PITX2 (show PITX2 Proteins) transcriptional activity.
Protein inhibitor of activated STAT (show STAT1 Proteins), PIASy regulates alpha-smooth muscle actin (show ACTG2 Proteins) expression by interacting with E12 (show ELSPBP1 Proteins) in mesangial cells.
PIASy negatively regulates both IFN transcription and IFN-stimulated gene expression through multiple mechanisms utilizing the function of different domains.
Studies define an important role of PIASy in hypoxia signaling through promoting HIF1alpha (show HIF1A Proteins) SUMOylation.
PIASgamma as a transcriptional co-regulator of Nurr1 (show NR4A2 Proteins) and suggest that this interaction may have a physiological role in regulating the expression of Nurr1 (show NR4A2 Proteins) target genes.
Piasy(-/-) mice appear phenotypically normal, activation of STAT1 (show STAT1 Proteins) is not significantly perturbed, and sumoylation patterns for SUMO-1 (show SUMO1 Proteins) or SUMO-3 (show SUMO3 Proteins) modification are similar in wild-type and knockout mice
post-translational modification of Nkx3.2 (show NKX3-2 Proteins) employing HDAC9 (show HDAC9 Proteins)-PIASy-RNF4 (show RNF4 Proteins) axis plays a crucial role in controlling chondrocyte viability and hypertrophic maturation during skeletal development in vertebrates.
these findings provide evidence for the effects of PIAsxalpha (show PIAS2 Proteins) and its mechanism on osteosarcoma progression, which offers novel insight into sumoylation and the cell cycle in osteosarcoma.
PIAS4 was identified as a candidate gene for abnormal head size in 13 patients with proximal 19p13.3 submicroscopic rearrangements .
Our data reveal a novel and dynamic role for PIAS4 in the cellular-mediated restriction of herpesviruses and establish a new functional role for the PIAS family of SUMO ligases in the intrinsic antiviral immune response to DNA virus infection.
PIAS4 activity are required for the AMPKalpha1 (show PRKAA1 Proteins) SUMOylation and the inhibition of AMPKalpha1 (show PRKAA1 Proteins) activity towards mTORC1 signalling.
PIAS4 (rs735842) and VEGFA (show VEGFA Proteins) (rs699947) were the most statistically significant variants associated in hypoxia pathway analysis.
PIASgamma-dependent modification of tomosyn-1 (show STXBP5 Proteins) with SUMO-2 (show SUMO2 Proteins)/3 presents a novel mechanism to adapt secretory strength to the dynamic synaptic environment.
SUMOylation of RXRalpha (show RXRA Proteins) is significantly enhanced through PIAS4-mediated activity.
High reactive oxygen speciesinduces oxidation and ubiquitin-mediated degradation of PIASgamma, thereby disrupting PIASgamma-IKKgamma (show IKBKG Proteins) cross talk.
Data suggest that PIASy exhibits a SIM (show SIM2 Proteins) (SUMO-interacting motif) in addition to the SIM (show SIM2 Proteins) identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy, and both are required for full ligase activity of PIASy; hydrophobic core residues of the new SIM (show SIM2 Proteins) are essential in binding to SUMO-3 (show SUMO3 Proteins). (PIASy = protein inhibitors of activated STAT (show STAT1 Proteins) y; SUMO-3 (show SUMO3 Proteins) = small ubiquitin-like modifier 3 (show SUMO3 Proteins))
The Xenopus PIAS (show PIAS1 Proteins) genes are expressed throughout early development and have overlapping and distinct expression patterns, with, for example, strong expression of PIAS4 in the neural and neural crest derivatives.
XPIASy functions as an essential negative regulator of the XSmad2 (show SMAD2 Proteins) pathway to ensure proper mesoderm induction at the appropriate time and in the appropriate region.
Data show that the Rod/Zw10 (show ZW10 Proteins) complex interacts with the first 47 residues of PIASy which are important for mitotic SUMOylation, and that depletion of Rod compromises the centromeric localization of PIASy and SUMO2 (show SUMO2 Proteins)/3 in mitosis.
a PIAS4 homologue (zfPIAS4a) from the zebrafish model that shares many conserved structural hallmarks with the human and mammal PIAS4 proteins was successfully identified
Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Promotes PARK7 sumoylation. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations.
protein inhibitor of activated STAT, 4
, protein inhibitor of activated STAT protein 4
, E3 SUMO-protein ligase PIAS4-like
, e3 SUMO-protein ligase PIAS4-like
, E3 SUMO-protein ligase PIAS4
, protein inhibitor of activated STAT PIASy
, protein inhibitor of activated STAT protein gamma
, protein inhibitor of activated STAT protein PIASy
, zinc finger, MIZ-type containing 6
, protein inhibitor of activated STAT 4