ArticleMolecular and cellular biology2004
PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 78 citations in OpenAlex.
- Structural diversity of p63 and p73 isoforms.Cell death and differentiation · 2022Review
- The Role of SUMO E3 Ligases in Signaling Pathway of Cancer Cells.International journal of molecular sciences · 2022Review
- PIAS Factors from Rainbow Trout Control NF-κB- and STAT-Dependent Gene Expression.International journal of molecular sciences · 2021Article
- The p53 family member p73 in the regulation of cell stress response.Biology direct · 2021Review
- Targeting Post-Translational Modifications of the p73 Protein: A Promising Therapeutic Strategy for Tumors.Cancers · 2021Review
- Su(var)2-10 and the SUMO Pathway Link piRNA-Guided Target Recognition to Chromatin Silencing.Molecular cell · 2020Article
- Circular Trajectory Reconstruction Uncovers Cell-Cycle Progression and Regulatory Dynamics from Single-Cell Hi-C Maps.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- PIAS1 is not suitable as a urothelial carcinoma biomarker protein and pharmacological target.PloS one · 2019Article
- p73 expression is regulated by ribosomal protein RPL26 through mRNA translation and protein stability.Oncotarget · 2016Article
- S100A6 Regulates Endothelial Cell Cycle Progression by Attenuating Antiproliferative Signal Transducers and Activators of Transcription 1 Signaling.Arteriosclerosis, thrombosis, and vascular biology · 2016Article
- Article
- A balancing act: orchestrating amino-truncated and full-length p73 variants as decisive factors in cancer progression.Oncogene · 2015Review
- PIAS1 is a crucial factor for prostate cancer cell survival and a valid target in docetaxel resistant cells.Oncotarget · 2014Article
- p53 Family and Cellular Stress Responses in Cancer.Frontiers in oncology · 2014Review
- Identification of a non-covalent ternary complex formed by PIAS1, SUMO1, and UBC9 proteins involved in transcriptional regulation.The Journal of biological chemistry · 2013Article
- p73 regulates autophagy and hepatocellular lipid metabolism through a transcriptional activation of the ATG5 gene.Cell death and differentiation · 2013Article
- Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNA.Nucleic acids research · 2013Article
- Regulation of p73 activity by post-translational modifications.Cell death & disease · 2012Review
- FLASH is essential during early embryogenesis and cooperates with p73 to regulate histone gene transcription.Oncogene · 2012Article
- Article
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p73 is a recently described member of the p53 family, and, like p53, it undergoes a number of posttranslational modifications. Here we show, by yeast two-hybrid screening, pull-down assays, and coimmunoprecipitation, that p73alpha, -beta, and -gamma bind to the protein inhibitor of activated STAT-1 (PIAS-1) and that this binding stabilizes p73. PIAS-1 also sumoylates p73alpha, although not the C-terminally truncated isoforms p73beta and -gamma, and this requires the RING finger domain of PIAS-1. The DeltaNp73alpha isoform can also bind, and be sumoylated by, PIAS-1. PIAS-1-mediated sumoylation decreases p73 transcriptional activity on several target promoters, such as Bax. p73 is colocalized in the nucleus with PIAS-1, and sumoylated p73 is located exclusively in the nuclear matrix. PIAS-1 is expressed predominantly during S phase, and PIAS-1 overexpression reduces p73-mediated transcription of p21, with a reduction of cells in G(1) and cell cycle reentry. Inhibition of endogenous PIAS-1 by RNA interference reduces the proportion of cells in S phase and induces G(2) arrest. These data suggest that PIAS-1, acting partly through binding and sumoylation of p73, is an important component of the cell cycle machinery.
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