Regulation of gene-activation pathways by PIAS proteins in the immune system

@article{Shuai2005RegulationOG,
  title={Regulation of gene-activation pathways by PIAS proteins in the immune system},
  author={Ke Shuai and Bin Liu},
  journal={Nature Reviews Immunology},
  year={2005},
  volume={5},
  pages={593-605}
}
  • K. ShuaiB. Liu
  • Published 1 August 2005
  • Biology
  • Nature Reviews Immunology
The protein inhibitor of activated STAT (PIAS) family of proteins has been proposed to regulate the activity of many transcription factors, including signal transducer and activator of transcription proteins (STATs), nuclear factor-κB, SMA- and MAD-related proteins (SMADs), and the tumour-suppressor protein p53. PIAS proteins regulate transcription through several mechanisms, including blocking the DNA-binding activity of transcription factors, recruiting transcriptional corepressors or co… 

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Identification of STAT3-independent regulatory effects for protein inhibitor of activated STAT3 by binding to novel transcription factors

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Protein Inhibitor of Activated STAT1 Interacts with and Up-regulates Activities of the Pro-proliferative Transcription Factor Krüppel-like Factor 5*

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The Role of Signal Transducer and Activator of Transcription 3 (STAT3) and Its Targeted Inhibition in Hematological Malignancies

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References

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PIAS/SUMO: new partners in transcriptional regulation

A model how the PIAS/ SUMO system may modulate transcriptional activities by mediating the assembly of coactivator or corepressor complexes within distinct subnuclear structures is proposed.

SUMO Modification of STAT1 and Its Role in PIAS-mediated Inhibition of Gene Activation*

It is demonstrated that STAT1 is a substrate for SUMO modification and that PIASx-α, but not PIAS1, functions as an E3 ligase to promote STAT1 modification, and that inhibition of STAT1 by PIAS proteins does not requiresumO modification ofSTAT1 itself.

Inhibition of Stat1-mediated gene activation by PIAS1.

  • B. LiuJ. Liao K. Shuai
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1998
The results identify PIAS1 as a specific inhibitor of Stat1-mediated gene activation and suggest that there may exist a specific PIAS inhibitor in every STAT signaling pathway.

Specific inhibition of Stat3 signal transduction by PIAS3.

Results indicate that PIAS3 is a specific inhibitor of Stat3, a signal transducer and activator of transcription-3 (Stat3) protein activated by the interleukin 6 family of cytokines, epidermal growth factor, and leptin.

Negative Regulation of NF-κB Signaling by PIAS1

It is reported here that PIAS1 (protein inhibitor of activated STAT1) is an important negative regulator of NF-κB, and microarray analysis indicates that the removal ofPIAS1 results in an increased expression of a subset of NF -κB-mediated genes in response to tumor necrosis factor alpha and lipopolysaccharide.

PIASx Is a Transcriptional Co-repressor of Signal Transducer and Activator of Transcription 4*

It is reported here that PIASx, a member of the protein inhibitor of activated STAT (PIAS) family, is a negative regulator of Stat4, a latent cytoplasmic transcription factor that becomes associated with Stat4 following IL-12 stimulation in vivo.

A transcriptional corepressor of Stat1 with an essential LXXLL signature motif

The studies identify PIASy as a transcriptional corepressor of Stat1 and suggest that different PIAS proteins may repress STAT-mediated gene activation through distinct mechanisms.

Modulation of STAT signaling by STAT-interacting proteins

The roles of STAT-interacting proteins in the regulation of STAT signaling are reviewed, finding a number of proteins function to modulate STAT signaling at various steps and mediate the crosstalk of STATs with other cellular signaling pathways.

Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)*

It is reported that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses, suggesting that PIAS1 is a novel activator of p 53.

PIAS proteins promote SUMO-1 conjugation to STAT1.

It is shown that STAT1 is subject to SUMO-1 modification, and sumoylation occurs in vivo and in vitro at a single, evolutionary conserved amino acid residue Lys703, and that PIAS proteins promote SUMo-1 conjugation to STAT1.
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