ArticleNucleic acids research2005
RGG-boxes of the EWS oncoprotein repress a range of transcriptional activation domains.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Heterogeneous Folding Intermediates Govern the Conformational Pathway of the RNA Recognition Motif Domain of the Ewing Sarcoma Protein.Biomolecules · 2025Article
- Molecular basis of EWS interdomain self-association and its role in condensate formation.Protein science : a publication of the Protein Society · 2025Article
- Review
- Article
- The FXR1 network acts as signaling scaffold for actomyosin remodeling.bioRxiv : the preprint server for biology · 2024Article
- Acetylation dependent translocation of EWSR1 regulates CHK2 alternative splicing in response to DNA damage.Oncogene · 2022Article
- Differential interaction of PRMT1 with RGG-boxes of the FET family proteins EWS and TAF15.Protein science : a publication of the Protein Society · 2018Article
- Lurbinectedin Inactivates the Ewing Sarcoma Oncoprotein EWS-FLI1 by Redistributing It within the Nucleus.Cancer research · 2016Article
- RGG boxes within the TET/FET family of RNA-binding proteins are functionally distinct.Transcription · 2016Article
- Ewing sarcoma protein: a key player in human cancer.International journal of cell biology · 2013Review
- Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.PLoS computational biology · 2013Article
- Structure of noncoding RNA is a determinant of function of RNA binding proteins in transcriptional regulation.Cell & bioscience · 2012Article
- Article
- Arginine methylation controls the subcellular localization and functions of the oncoprotein splicing factor SF2/ASF.Molecular and cellular biology · 2010Article
- SOLO: a meiotic protein required for centromere cohesion, coorientation, and SMC1 localization in Drosophila melanogaster.The Journal of cell biology · 2010Article
- The TET family of proteins: functions and roles in disease.Journal of molecular cell biology · 2009Review
- In vitro interaction between the N-terminus of the Ewing's sarcoma protein and the subunit of RNA polymerase II hsRPB7.Molecular biology reports · 2009Article
- EppA, a putative substrate of DdERK2, regulates cyclic AMP relay and chemotaxis in Dictyostelium discoideum.Eukaryotic cell · 2006Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Ewings Sarcoma Oncoprotein (EWS) interacts with several components of the mammalian transcriptional and pre-mRNA splicing machinery and is also found in the cytoplasm and even on the cell surface. The apparently diverse cellular functions of EWS are, however, not well characterized. EWS harbours a potent N-terminal transcriptional activation domain (the EAD) that is revealed in the context of oncogenic EWS-fusion proteins (EFPs) and a C-terminal RNA-binding domain (RBD) that recruits pre-mRNA splicing factors and may couple transcription and splicing. In contrast to EFPs, the presumed transcriptional role of normal EWS remains enigmatic. Here, we report that multiple RGG-boxes within the RBD are necessary and sufficient for cis-repression of the EAD and that RGG-boxes can also repress in-trans, within dimeric partners. Lys can functionally substitute for Arg, indicating that the basic nature of the Arg side chain is the critical determinant of RGG-box-mediated repression. In addition to the EAD, RGG-boxes can repress a broad range of activation domains (including those of VP16, E1a and CREB), but repression can be alleviated by the simultaneous presence of more than one activation domain. We therefore propose that a key function of RGG boxes within native EWS is to restrict promiscuous activation by the EAD while still allowing EWS to enter functional transcription complexes and participate in other transactions involving pre-mRNAs.
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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.