ArticleOncogene2007
Regulation of the Ets-1 transcription factor by sumoylation and ubiquitinylation.
Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The trial behind it
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Who cites it
37 citing papers in PubMed.
- ETS1-EGR2 facilitates renal cell carcinoma progression by activating NOTCH signalling.Clinical and translational medicine · 2026Article
- Melatonin Suppresses NLRP3 Inflammasome Activation via SIRT1-Mediated ETS1 Deacetylation to Attenuate LPS-Induced Pyroptosis in Alveolar Epithelial Cells.Journal of inflammation research · 2026Article
- The silence within: a conserved intragenic silencing element governs HTLV-1 expression via host RUNX1 complex binding.Npj viruses · 2025Article
- The Dynamic Regulation of Daxx-Mediated Transcriptional Inhibition by SUMO and PML NBs.International journal of molecular sciences · 2025Review
- Versatile roles of disordered transcription factor effector domains in transcriptional regulation.The FEBS journal · 2025Review
- Central role of SUMOylation in the regulation of chromatin interactions and transcriptional outputs of the androgen receptor in prostate cancer cells.Nucleic acids research · 2024Article
- ETS1 Function in Leukemia and Lymphoma.Advances in experimental medicine and biology · 2024Review
- Tissue-specific inhibition of protein sumoylation uncovers diverse SUMO functions during C. elegans vulval development.PLoS genetics · 2022Article
- An integrated multi-omic analysis of iPSC-derived motor neurons from C9ORF72 ALS patients.iScience · 2021Article
- Ubiquitin-Mediated Control of ETS Transcription Factors: Roles in Cancer and Development.International journal of molecular sciences · 2021Review
- The SUMO-specific protease SENP1 deSUMOylates p53 and regulates its activity.Journal of cellular biochemistry · 2021Article
- HUWE1 Causes an Immune Imbalance in Immune Thrombocytopenic Purpura by Reducing the Number and Function of Treg Cells Through the Ubiquitination Degradation of Ets-1.Frontiers in cell and developmental biology · 2021Article
- SUMOylation of the transcription factor ZFHX3 at Lys-2806 requires SAE1, UBC9, and PIAS2 and enhances its stability and function in cell proliferation.The Journal of biological chemistry · 2020Article
- Writing and erasing MYC ubiquitination and SUMOylation.Genes & diseases · 2019Review
- A deficiency in SUMOylation activity disrupts multiple pathways leading to neural tube and heart defects in Xenopus embryos.BMC genomics · 2019Article
- Transcription Factor ETS-1 and Reactive Oxygen Species: Role in Vascular and Renal Injury.Antioxidants (Basel, Switzerland) · 2018Review
- A genetic screen to discover SUMOylated proteins in living mammalian cells.Scientific reports · 2017Article
- Usp9x regulates Ets-1 ubiquitination and stability to control NRAS expression and tumorigenicity in melanoma.Nature communications · 2017Article
- Proteasomal Degradation of the EWS-FLI1 Fusion Protein Is Regulated by a Single Lysine Residue.The Journal of biological chemistry · 2016Article
- SUMO wrestling with Ras.Small GTPases · 2016Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sumoylation and ubiquitinylation reversibly regulate the activity of transcription factors through covalent attachment to lysine residues of target proteins. We examined whether the Ets-1 transcription factor is modified by sumoylation and/or ubiquitinylation. Among four potential SUMO motifs in Ets-1, we identified lysines 15 and 227 within the LK(15)YE and IK(227)QE motifs, as being the sumoylation acceptor sites. Using transfection of Ets-1 wildtype (WT) or its sumoylation deficient version (Ets-1 K15R/K227R), as well as WT or mutant proteins of the SUMO pathway, we further demonstrated that the E2 SUMO-conjugating enzyme Ubc9 and a E3 SUMO ligase, PIASy, can enhance Ets-1 sumoylation, while a SUMO protease, SENP1, can desumoylate Ets-1. We also found that Ets-1 is modified by K48-linked polyubiquitinylation independently of the sumoylation acceptor sites and is degraded through the 26S proteasome pathway, while sumoylation of Ets-1 does not affect its stability. Finally, sumoylation of Ets-1 leads to reduced transactivation and we demonstrated that previously identified critical lysine residues in Synergistic Control motifs are the sumoylation acceptor sites of Ets-1. These data show that Ets-1 can be modified by sumoylation and/or ubiquitinylation, with sumoylation repressing transcriptional activity of Ets-1 and having no clear antagonistic action on the ubiquitin-proteasome degradation pathway.
Indexed as
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.