ArticleHuman molecular genetics2009
Discrimination of common and unique RNA-binding activities among Fragile X mental retardation protein paralogs.
Article in Human molecular genetics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 169 citations in OpenAlex.
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences.International journal of molecular sciences · 2025Review
- FXR1 associates with and degrades PDZK1IP1 and ATOH8 mRNAs and promotes esophageal cancer progression.Biology direct · 2024Article
- An in-depth review of the function of RNA-binding protein FXR1 in neurodevelopment.Cell and tissue research · 2024Review
- PRMT5-mediated arginine methylation of FXR1 is essential for RNA binding in cancer cells.Nucleic acids research · 2024Article
- FMRP-mediated spatial regulation of physiologic NMD targets in neuronal cells.Genome biology · 2024Review
- FMRP cooperates with miRISC components to repress translation and regulate neurite morphogenesis inRNA biology · 2024Article
- Characterization of Fragile X Mental Retardation Protein expression in human nociceptors and their axonal projections to the spinal dorsal horn.The Journal of comparative neurology · 2023Article
- Fragile X-Related Protein FXR1 Controls Human Adenovirus Capsid mRNA Metabolism.Journal of virology · 2023Article
- Increased Serum Levels of miR-125b and miR-132 in Fragile X Syndrome: A Preliminary Study.Neurology. Genetics · 2022Article
- Exosomal circZNF451 restrains anti-PD1 treatment in lung adenocarcinoma via polarizing macrophages by complexing with TRIM56 and FXR1.Journal of experimental & clinical cancer research : CR · 2022Article
- The Fragile X Protein Disordered Regions Bind a Novel RNA Target.Biochemistry · 2022Article
- Fmr1 exon 14 skipping in late embryonic development of the rat forebrain.BMC neuroscience · 2022Article
- FXS causing missense mutations disrupt FMRP granule formation, dynamics, and function.PLoS genetics · 2022Article
- The Fragile X Proteins Differentially Regulate Translation of Reporter mRNAs with G-quadruplex Structures.Journal of molecular biology · 2022Article
- Combining affinity purification and mass spectrometry to define the network of the nuclear proteins interacting with the N-terminal region of FMRP.Frontiers in molecular biosciences · 2022Article
- FXR1 regulation of parvalbumin interneurons in the prefrontal cortex is critical for schizophrenia-like behaviors.Molecular psychiatry · 2021Article
- A serum microRNA sequence reveals fragile X protein pathology in amyotrophic lateral sclerosis.Brain : a journal of neurology · 2021Article
- Absence of RNA-binding protein FXR2P prevents prolonged phase of kainate-induced seizures.EMBO reports · 2021Article
- The molecular biology of FMRP: new insights into fragile X syndrome.Nature reviews. Neuroscience · 2021Review
15 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Fragile X mental retardation is caused by loss-of-function of a single gene encoding FMRP, an RNA-binding protein that harbors three canonical RNA-binding domains, two KH-type and one RGG box. Two autosomal paralogs of FMRP, FXR1P and FXR2P, are similar to FMRP in their overall structure, including the presence of putative RNA-binding domains, but to what extent they provide functional redundancy with FMRP is unclear. Although FMRP has been characterized as a polyribosome-associated regulator of translation, less is known about the functions of FXR1P and FXR2P. For example, FMRP binds intramolecular G-quadruplex and kissing complex RNA (kcRNA) ligands via the RGG box and KH2 domain, respectively, although the RNA ligands of FXR1P and FXR2P are unknown. Here we demonstrate that FXR1P and FXR2P KH2 domains bind kcRNA ligands with the same affinity as the FMRP KH2 domain although other KH domains do not. RNA ligand recognition by this family is highly conserved, as the KH2 domain of the single Drosophila ortholog, dFMRP, also binds kcRNA. kcRNA was able to displace FXR1P and FXR2P from polyribosomes as it does for FMRP, and this displacement was FMRP-independent. This suggests that all three family members recognize the same binding site on RNA mediating their polyribosome association, and that they may be functionally redundant with regard to this aspect of translational control. In contrast, FMRP is unique in its ability to recognize G-quadruplexes, suggesting the FMRP RGG domain may play a non-redundant role in the pathophysiology of the disease.
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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.