ArticlePloS one2007
Nitric oxide destabilizes Pias3 and regulates sumoylation.
Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 44 citations in OpenAlex.
- Updates on the role of TRIM proteins in AIDS: molecular mechanisms and potential for interventions.Frontiers in immunology · 2026Review
- The impact of nitric oxide on HER family post-translational modification and downstream signaling in cancer.Frontiers in physiology · 2024Review
- Precision Redox: The Key for Antioxidant Pharmacology.Antioxidants & redox signaling · 2021Review
- Nucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration.International journal of molecular sciences · 2021Review
- Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading.Frontiers in physiology · 2019Article
- Post-transcriptional regulation of PIAS3 expression by miR-18a in malignant mesothelioma.Molecular oncology · 2018Article
- Nuclear Smad6 promotes gliomagenesis by negatively regulating PIAS3-mediated STAT3 inhibition.Nature communications · 2018Article
- A charge-sensing region in the stromal interaction molecule 1 luminal domain confers stabilization-mediated inhibition of SOCE in response toThe Journal of biological chemistry · 2018Article
- Protein Inhibitor of Activated STAT3 Suppresses Oxidized LDL-induced Cell Responses during Atherosclerosis in Apolipoprotein E-deficient Mice.Scientific reports · 2016Article
- Ubiquitin-Conjugating Enzyme 9 Phosphorylation as a Novel Mechanism for Potentiation of the Inflammatory Response.The American journal of pathology · 2016Article
- Protein Inhibitor of Activated STAT3 (PIAS3) Is Down-Regulated in Eutopic Endometrium of Women with Endometriosis.Biology of reproduction · 2016Article
- SNOs Differ: Methodological and Biological Implications.Circulation research · 2015Article
- Lipopolysaccharides Promote S-Nitrosylation and Proteasomal Degradation of Liver Kinase B1 (LKB1) in Macrophages in Vivo.The Journal of biological chemistry · 2015Article
- SUMOylation occurs in acute kidney injury and plays a cytoprotective role.Biochimica et biophysica acta · 2015Article
- SUMO rules: regulatory concepts and their implication in neurologic functions.Neuromolecular medicine · 2013Review
- Gating neural development and aging via nuclear pores.Cell research · 2012Article
- Regulation by S-nitrosylation of protein post-translational modification.The Journal of biological chemistry · 2012Review
- The role of small ubiquitin-like modifier-interacting motif in the assembly and regulation of metal-responsive transcription factor 1.The Journal of biological chemistry · 2011Article
- Xanthine oxidoreductase promotes the inflammatory state of mononuclear phagocytes through effects on chemokine expression, peroxisome proliferator-activated receptor-{gamma} sumoylation, and HIF-1{alpha}.The Journal of biological chemistry · 2011Article
- Comprehensively surveying structure and function of RING domains from Drosophila melanogaster.PloS one · 2011Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small ubiquitin-related protein modifiers (SUMO) modification is an important mechanism for posttranslational regulation of protein function. However, it is largely unknown how the sumoylation pathway is regulated. Here, we report that nitric oxide (NO) causes global hyposumoylation in mammalian cells. Both SUMO E2 conjugating enzyme Ubc9 and E3 ligase protein inhibitor of activated STAT3 (Pias3) were targets for S-nitrosation. S-nitrosation did not interfere with the SUMO conjugating activity of Ubc9, but promoted Pias3 degradation by facilitating its interaction with tripartite motif-containing 32 (Trim32), a ubiquitin E3 ligase. On the one hand, NO promoted Trim32-mediated Pias3 ubiquitination. On the other hand, NO enhanced the stimulatory effect of Pias3 on Trim32 autoubiquitination. The residue Cys459 of Pias3 was identified as a target site for S-nitrosation. Mutation of Cys459 abolished the stimulatory effect of NO on the Pias3-Trim32 interaction, indicating a requirement of S-nitrosation at Cys459 for positive regulation of the Pias3-Trim32 interplay. This study reveals a novel crosstalk between S-nitrosation, ubiquitination, and sumoylation, which may be crucial for NO-related physiological and pathological processes.
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