دورية أكاديمية
أعرض في EDS

ERG transcription factors have a splicing regulatory function involving RBFOX2 that is altered in the EWS-FLI1 oncogenic fusion.

التفاصيل البيبلوغرافية
العنوان: ERG transcription factors have a splicing regulatory function involving RBFOX2 that is altered in the EWS-FLI1 oncogenic fusion.
المؤلفون: Saulnier O; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France.; Université Paris Diderot, Sorbonne Paris Cité, F-75013 Paris, France., Guedri-Idjouadiene K; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Aynaud MM; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Chakraborty A; Institut Curie, PSL Research University, CNRS UMR3348, INSERM U1278, F-91405 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, INSERM U1278, F-91405 Orsay, France.; Équipe Labellisée Ligue Nationale Contre le Cancer, F-91405 Orsay, France., Bruyr J; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Pineau J; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., O'Grady T; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Mirabeau O; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Grossetête S; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Galvan B; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Claes M; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Al Oula Hassoun Z; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Sadacca B; INSERM U932, RT2Lab Team, Translational Research Department, PSL Research University, Institut Curie, F-75005 Paris, France.; CNRS UMR5219, Institut de Mathématiques de Toulouse; Université de Toulouse; F-31062 Toulouse, France., Laud K; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Zaïdi S; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Surdez D; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Baulande S; Institut Curie, PSL Research University, NGS Platform, 26 rue d'Ulm, F-75005 Paris, France., Rambout X; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium., Tirode F; Claude Bernard University Lyon 1, INSERM 1052, CNRS 5286, Cancer Research Center of Lyon (CRCL), Lyon University, Lyon, France., Dutertre M; Institut Curie, PSL Research University, CNRS UMR3348, INSERM U1278, F-91405 Orsay, France.; Université Paris-Saclay, CNRS UMR3348, INSERM U1278, F-91405 Orsay, France.; Équipe Labellisée Ligue Nationale Contre le Cancer, F-91405 Orsay, France., Delattre O; INSERM U830, Équipe Labellisée LNCC, PSL Research University, SIREDO Oncology Centre, Institut Curie, 75005 Paris, France., Dequiedt F; University of Liège, Interdisciplinary Cluster for Applied Genoproteomics (GIGA), Liège, Belgium.; University of Liège, GIGA-Molecular Biology of Diseases, Liège, Belgium.
المصدر: Nucleic acids research [Nucleic Acids Res] 2021 May 21; Vol. 49 (9), pp. 5038-5056.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Oxford University Press Country of Publication: England NLM ID: 0411011 Publication Model: Print Cited Medium: Internet ISSN: 1362-4962 (Electronic) Linking ISSN: 03051048 NLM ISO Abbreviation: Nucleic Acids Res Subsets: MEDLINE
أسماء مطبوعة: Publication: 1992- : Oxford : Oxford University Press
Original Publication: London, Information Retrieval ltd.
مواضيع طبية MeSH: Alternative Splicing*, Oncogene Proteins, Fusion/*metabolism , Proto-Oncogene Protein c-fli-1/*metabolism , RNA Splicing Factors/*metabolism , RNA-Binding Protein EWS/*metabolism , Repressor Proteins/*metabolism, Calmodulin-Binding Proteins/genetics ; Calmodulin-Binding Proteins/metabolism ; Cell Line ; Cell Line, Tumor ; HeLa Cells ; Human Umbilical Vein Endothelial Cells/metabolism ; Humans ; Protein Domains ; Sarcoma, Ewing/genetics ; Sarcoma, Ewing/metabolism ; Transcriptional Regulator ERG/chemistry ; Transcriptional Regulator ERG/metabolism
مستخلص: ERG family proteins (ERG, FLI1 and FEV) are a subfamily of ETS transcription factors with key roles in physiology and development. In Ewing sarcoma, the oncogenic fusion protein EWS-FLI1 regulates both transcription and alternative splicing of pre-messenger RNAs. However, whether wild-type ERG family proteins might regulate splicing is unknown. Here, we show that wild-type ERG proteins associate with spliceosomal components, are found on nascent RNAs, and induce alternative splicing when recruited onto a reporter minigene. Transcriptomic analysis revealed that ERG and FLI1 regulate large numbers of alternative spliced exons (ASEs) enriched with RBFOX2 motifs and co-regulated by this splicing factor. ERG and FLI1 are associated with RBFOX2 via their conserved carboxy-terminal domain, which is present in EWS-FLI1. Accordingly, EWS-FLI1 is also associated with RBFOX2 and regulates ASEs enriched in RBFOX2 motifs. However, in contrast to wild-type ERG and FLI1, EWS-FLI1 often antagonizes RBFOX2 effects on exon inclusion. In particular, EWS-FLI1 reduces RBFOX2 binding to the ADD3 pre-mRNA, thus increasing its long isoform, which represses the mesenchymal phenotype of Ewing sarcoma cells. Our findings reveal a RBFOX2-mediated splicing regulatory function of wild-type ERG family proteins, that is altered in EWS-FLI1 and contributes to the Ewing sarcoma cell phenotype.
(© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.)
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المشرفين على المادة: 0 (ADD3 protein, human)
0 (Calmodulin-Binding Proteins)
0 (ERG protein, human)
0 (EWS-FLI fusion protein)
0 (FLI1 protein, human)
0 (Oncogene Proteins, Fusion)
0 (Proto-Oncogene Protein c-fli-1)
0 (RBFOX2 protein, human)
0 (RNA Splicing Factors)
0 (RNA-Binding Protein EWS)
0 (Repressor Proteins)
0 (Transcriptional Regulator ERG)
تواريخ الأحداث: Date Created: 20210519 Date Completed: 20210706 Latest Revision: 20210706
رمز التحديث: 20221213
مُعرف محوري في PubMed: PMC8136815
DOI: 10.1093/nar/gkab305
PMID: 34009296
قاعدة البيانات: MEDLINE
الوصف
تدمد:1362-4962
DOI:10.1093/nar/gkab305