ArticleThe Journal of biological chemistry2013
Covalent small ubiquitin-like modifier (SUMO) modification of Maf1 protein controls RNA polymerase III-dependent transcription repression.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Aurora-A-mediated cytosolic localization of Maf1 promotes cell proliferation via regulating mitochondrial function in HCC.Cell death discovery · 2025Article
- Maf1 cooperates with progesterone receptor to repress RNA polymerase III transcription of select tRNAs.Nucleic acids research · 2025Article
- Characterizing the differential distribution and targets of Sumo1 and Sumo2 in the mouse brain.iScience · 2023Article
- Sumoylation regulates functional properties of the oocyte transcription factors SOHLH1 and NOBOX.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- TransPhos: A Deep-Learning Model for General Phosphorylation Site Prediction Based on Transformer-Encoder Architecture.International journal of molecular sciences · 2022Article
- SUMO and Transcriptional Regulation: The Lessons of Large-Scale Proteomic, Modifomic and Genomic Studies.Molecules (Basel, Switzerland) · 2021Review
- Roles for the RNA polymerase III regulator MAFR-1 in regulating sperm quality in Caenorhabditis elegans.Scientific reports · 2020Article
- SUMOylation down-regulates rDNA transcription by repressing expression of upstream-binding factor and proto-oncogene c-Myc.The Journal of biological chemistry · 2019Article
- The RNA polymerase III repressor MAF1 is regulated by ubiquitin-dependent proteasome degradation and modulates cancer drug resistance and apoptosis.The Journal of biological chemistry · 2019Article
- Loss of the E2 SUMO-conjugating enzymeDevelopment (Cambridge, England) · 2019Article
- Defective RNA polymerase III is negatively regulated by the SUMO-Ubiquitin-Cdc48 pathway.eLife · 2018Article
- Signaling to and from the RNA Polymerase III Transcription and Processing Machinery.Annual review of biochemistry · 2018Review
- The C-Box Region of MAF1 Regulates Transcriptional Activity and Protein Stability.Journal of molecular biology · 2017Article
- Maf1, A New PTEN Target Linking RNA and Lipid Metabolism.Trends in endocrinology and metabolism: TEM · 2016Review
- Human MAF1 targets and represses active RNA polymerase III genes by preventing recruitment rather than inducing long-term transcriptional arrest.Genome research · 2016Article
- Emerging Roles for Maf1 beyond the Regulation of RNA Polymerase III Activity.Journal of molecular biology · 2015Review
- Sumoylation of Rap1 mediates the recruitment of TFIID to promote transcription of ribosomal protein genes.Genome research · 2015Article
- Arabidopsis HFR1 is a potential nuclear substrate regulated by the Xanthomonas type III effector XopD(Xcc8004).PloS one · 2015Article
- Sumo and the cellular stress response.Cell division · 2015Review
- Physiological roles for mafr-1 in reproduction and lipid homeostasis.Cell reports · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
RNA polymerase (pol) III transcribes genes that determine biosynthetic capacity. Induction of these genes is required for oncogenic transformation. The transcriptional repressor, Maf1, plays a central role in the repression of these and other genes that promote oncogenesis. Our studies identify an important new role for SUMOylation in repressing RNA pol III-dependent transcription. We show that a key mechanism by which this occurs is through small ubiquitin-like modifier (SUMO) modification of Maf1 by both SUMO1 and SUMO2. Mutation of each lysine residue revealed that Lys-35 is the major SUMOylation site on Maf1 and that the deSUMOylase, SENP1, is responsible for controlling Maf1K35 SUMOylation. SUMOylation of Maf1 is unaffected by rapamycin inhibition of mammalian target of rapamycin (mTOR) and mTOR-dependent Maf1 phosphorylation. By preventing SUMOylation at Lys-35, Maf1 is impaired in its ability to both repress transcription and suppress colony growth. Although SUMOylation does not alter Maf1 subcellular localization, Maf1K35R is defective in its ability to associate with RNA pol III. This impairs Maf1 recruitment to tRNA gene promoters and its ability to facilitate the dissociation of RNA pol III from these promoters. These studies identify a novel role for SUMOylation in controlling Maf1 and RNA pol III-mediated transcription. Given the emerging roles of SENP1, Maf1, and RNA pol III transcription in oncogenesis, our studies support the idea that deSUMOylation of Maf1 and induction of its gene targets play a critical role in cancer development.
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