ArticleNucleic acids research2009
FRAXE-associated mental retardation protein (FMR2) is an RNA-binding protein with high affinity for G-quartet RNA forming structure.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 86 citations in OpenAlex.
- All hands on DEK: structural insights into a unique histone modifier and chromatin remodeler.Epigenetics & chromatin · 2026Review
- Molecular insight into transcriptome profiling of aerobic exercise induced changes in aged skeletal muscle.npj aging · 2026Article
- Molecular evolution of transcription factors AF4/FMR2 family member (AFF) gene family and the role of lamprey AFF3 in cell proliferation.Development genes and evolution · 2024Article
- An intragenic duplication in the AFF2 gene associated with Cornelia de Lange syndrome phenotype.Frontiers in genetics · 2024Article
- Advances in the discovery and analyses of human tandem repeats.Emerging topics in life sciences · 2023Review
- Unravelling the link between neurodevelopmental disorders and short tandem CGG-repeat expansions.Emerging topics in life sciences · 2023Review
- In Silico Identification of Potential Quadruplex Forming Sequences in LncRNAs of Cervical Cancer.International journal of molecular sciences · 2023Article
- The impact of the chromatin binding DEK protein in hematopoiesis and acute myeloid leukemia.Experimental hematology · 2023Review
- Translocations and Gene Fusions in Sinonasal Malignancies.Current oncology reports · 2023Review
- A novel WWTR1::AFF2 fusion in an intra-abdominal soft tissue sarcoma with associated endometriosis.Genes, chromosomes & cancer · 2022Article
- G-Quadruplex-Binding Proteins: Promising Targets for Drug Design.Biomolecules · 2022Review
- A novel LARGE1-AFF2 fusion expanding the molecular alterations associated with the methylation class of neuroepithelial tumors with PATZ1 fusions.Acta neuropathologica communications · 2022Article
- Article
- DEK-AFF2 fusion-associated papillary squamous cell carcinoma of the sinonasal tract: clinicopathologic characterization of seven cases with deceptively bland morphology.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2021Article
- Properties and biological impact of RNA G-quadruplexes: from order to turmoil and back.Nucleic acids research · 2020Article
- Fused in sarcoma silences HIV gene transcription and maintains viral latency through suppressing AFF4 gene activation.Retrovirology · 2019Article
- Complete Disruption of Autism-Susceptibility Genes by Gene Editing Predominantly Reduces Functional Connectivity of Isogenic Human Neurons.Stem cell reports · 2018Article
- Novel in-frame deletion in MFSD8 gene revealed by trio whole exome sequencing in an Iranian affected with neuronal ceroid lipofuscinosis type 7: a case report.Journal of medical case reports · 2018Article
- Comprehensive identification of proteins binding to RNA G-quadruplex motifs in the 5' UTR of tumor-associated mRNAs.Biochimie · 2018Article
- Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions.Molecules (Basel, Switzerland) · 2017Review
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
FRAXE is a form of mild to moderate mental retardation due to the silencing of the FMR2 gene. The cellular function of FMR2 protein is presently unknown. By analogy with its homologue AF4, FMR2 was supposed to have a role in transcriptional regulation, but robust evidences supporting this hypothesis are lacking. We observed that FMR2 co-localizes with the splicing factor SC35 in nuclear speckles, the nuclear regions where splicing factors are concentrated, assembled and modified. Similarly to what was reported for splicing factors, blocking splicing or transcription leads to the accumulation of FMR2 in enlarged, rounded speckles. FMR2 is also localized in the nucleolus when splicing is blocked. We show here that FMR2 is able to specifically bind the G-quartet-forming RNA structure with high affinity. Remarkably, in vivo, in the presence of FMR2, the ESE action of the G-quartet situated in mRNA of an alternatively spliced exon of a minigene or of the putative target FMR1 appears reduced. Interestingly, FMR1 is silenced in the fragile X syndrome, another form of mental retardation. All together, our findings strongly suggest that FMR2 is an RNA-binding protein, which might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure.
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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.