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Protein inhibitor of activated STAT, 3

PIAS3, protein inhibitor of activated STAT3
This gene encodes a member of the PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)] family of transcriptional modulators. The protein functions as a SUMO (small ubiquitin-like modifier)-E3 ligase which catalyzes the covalent attachment of a SUMO protein to specific target substrates. It directly binds to several transcription factors and either blocks or enhances their activity. Alternatively spliced transcript variants of this gene have been identified, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: STAT3, Smt3, CAN, Ubiquitin, Interleukin-6
Papers on PIAS3
Correlation Between the Expression of MicroRNA-301a-3p and the Proportion of Th17 Cells in Patients with Rheumatoid Arthritis.
Wang et al., Zhenjiang, China. In Inflammation, Feb 2016
We also observed that the expression of protein inhibitor of activated STAT3 (PIAS3), the main cellular inhibitor of STAT3, was attenuated in RA patients and negatively correlated with the percentage of Th17 cells in RA.
PIAS3 enhances the transcriptional activity of HIF-1α by increasing its protein stability.
Kobayashi et al., Sapporo, Japan. In Biochem Biophys Res Commun, Feb 2016
In this study, we investigated the effects of protein inhibitor of activated STAT3 (PIAS3), a small ubiquitin-related modifier (SUMO) E3 ligase, on HIF-1-mediated transcriptional activation.
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.
The SUMO (Small Ubiquitin-like Modifier) Ligase PIAS3 Primes ATR for Checkpoint Activation.
Zou et al., Boston, United States. In J Biol Chem, Feb 2016
Here, we show that the PIAS3 SUMO ligase is important for activation of the ATR (ataxia telangiectasia and Rad3 related)-regulated DNA damage signaling pathway.
The ubiquitin ligase Smurf2 suppresses TGFβ-induced epithelial-mesenchymal transition in a sumoylation-regulated manner.
Bonni et al., Calgary, Canada. In Cell Death Differ, Jan 2016
We find that the SUMO-E2 conjugating enzyme Ubc9 and the SUMO E3 ligase PIAS3 associate with Smurf2 and promote its sumoylation at the distinct sites of Lysines 26 and 369.
PIAS3, SHP2 and SOCS3 Expression patterns in Cervical Cancers: Relevance with activation and resveratrol-caused inactivation of STAT3 signaling.
Liu et al., Dalian, China. In Gynecol Oncol, Dec 2015
SHP2, PIAS3, and SOCS3 are STAT3 negative regulators; therefore, their statuses in cervical adenocarcinoma (HeLa) and squamous cell carcinoma (SiHa and C33A) cell lines without and with resveratrol treatment and their correlation with STAT3 activation in CC specimens were investigated.
Prognostic value of protein inhibitor of activated STAT3 in breast cancer patients receiving hormone therapy.
Yeh et al., Kao-hsiung, Taiwan. In Bmc Cancer, Dec 2015
Alterations in specific negative regulators, such as protein inhibitor of activated STAT3 (PIAS3), may contribute to cancer development.
Regulatory network analysis of transcription factors, microRNAs, target genes and host genes in human multiple myeloma.
Wang et al., Changchun, China. In Pak J Pharm Sci, Nov 2015
For example, STAT3 and hsa-miR-125b, PIAS3 and hsa-miR-21 respectively formed self adaptation feedback regulations.
Interplay between microRNAs and the STAT3 signaling pathway in human cancers.
Huang et al., Nanchang, China. In Physiol Genomics, 2014
Some miRNAs directly modulate STAT3 activity through targeting the STAT3 3'-UTR; other miRNAs target SOCS, PIAS3, and EGFR genes, which encode proteins that regulate the STAT3 signaling pathway.
Protein inhibitor of activated STAT3 (PIAS3) protein promotes SUMOylation and nuclear sequestration of the intracellular domain of ErbB4 protein.
Elenius et al., Turku, Finland. In J Biol Chem, 2012
PIAS3 is a novel regulator of ErbB4 receptor tyrosine kinase, controlling its nuclear sequestration and function.
NF-κB repression by PIAS3 mediated RelA SUMOylation.
Kulesz-Martin et al., Portland, United States. In Plos One, 2011
NF-kappaB is regulated through a novel negative feedback mechanism by SUMOylation, where the RelA subunit of NF-kappaB is SUMOylated by PIAS3.
The PINIT domain of PIAS3: structure-function analysis of its interaction with STAT3.
Blatch et al., Grahamstown, South Africa. In J Mol Recognit, 2011
L97A, R99N and R99Q mutations of the PINIT domain (PIAS3(85-272) ) were found to abrogate binding to STAT3, suggesting that these residues were part of a potential binding surface.
Regulation of melanocyte pivotal transcription factor MITF by some other transcription factors.
He et al., Kunming, China. In Mol Cell Biochem, 2011
Activated signal transducer and activator of transcription 3 (STAT3) and protein inhibitor of activated STAT3 (PIAS3) are able to regulate transcriptional activity of MITF through their interaction.
Identification of STAT3-independent regulatory effects for protein inhibitor of activated STAT3 by binding to novel transcription factors.
Dowlati et al., Cleveland, United States. In Cancer Biol Ther, 2011
novel transcription factor binding partners for PIAS3 including ETS, EGR1, NR1I2, and GATA1 were identified.
Protein inhibitor of activated STAT3 expression in lung cancer.
Dowlati et al., Cleveland, United States. In Mol Oncol, 2011
Squamous cell carcinoma of the lung commonly lacks PIAS3 protein expression.
SUMOylation of the GTPase Rac1 is required for optimal cell migration.
Malliri et al., Manchester, United Kingdom. In Nat Cell Biol, 2010
Here, we identify that the small ubiquitin-like modifier (SUMO) E3-ligase, PIAS3, interacts with Rac1 and is required for increased Rac activation and optimal cell migration in response to hepatocyte growth factor (HGF) signalling.
The enigma of the role of protein inhibitor of activated STAT3 (PIAS3) in the immune response.
Razin et al., Jerusalem, Israel. In Trends Immunol, 2010
Protein inhibitor of activated STAT3 (PIAS3), the main cellular inhibitor of signal transducers and activator of transcription 3 (STAT3), has been described as a modulator of DNA binding transcription factors.
SUMO weighs in on a photoreceptor finish.
LaBonne, In Dev Cell, 2009
In a recent issue of Neuron, Onishi et al. show that PIAS3-mediated SUMOylation of Nr2e3 plays an essential role in the specification of rod photoreceptors by converting Nr2e3 to a potent repressor of cone gene expression.
The function of MITF and associated proteins in mast cells.
Razin et al., Jerusalem, Israel. In Mol Immunol, 2002
A search for MITF-associated proteins, using a mast cell library that was screened with a construct that encodes the basic helix-loop-helix leucine zipper (bHLH-Zip) domain of MITF, resulted in the isolation of the protein kinase C interacting (PKCI) protein 1 and protein inhibitor of activated STAT3 (PIAS3).
Specific inhibition of Stat3 signal transduction by PIAS3.
Shuai et al., Los Angeles, United States. In Science, 1998
A protein named PIAS3 (protein inhibitor of activated STAT) that binds to Stat3 was isolated and characterized.
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