ArticleMolecular biology of the cell2009
Cells lacking the fragile X mental retardation protein (FMRP) have normal RISC activity but exhibit altered stress granule assembly.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 95 citations in OpenAlex.
- RNA Granules at the Crossroads of Synaptic Dysfunction and Neurodegeneration.Journal of neurochemistry · 2025Review
- Computational investigation of the sequence context of arginine/glycine-rich motifs in the human proteome.BMC genomics · 2025Article
- The multifaceted role of Fragile X-Related Protein 1 (FXR1) in cellular processes: an updated review on cancer and clinical applications.Cell death & disease · 2024Review
- The Fragile X Protein Family in Amyotrophic Lateral Sclerosis.Molecular neurobiology · 2023Review
- A little less aggregation a little more replication: Viral manipulation of stress granules.Wiley interdisciplinary reviews. RNA · 2023Review
- The Fragile X Protein Disordered Regions Bind a Novel RNA Target.Biochemistry · 2022Article
- RNA-binding FMRP and Staufen sequentially regulate the Coracle scaffold to control synaptic glutamate receptor and bouton development.Development (Cambridge, England) · 2022Article
- Collective Learnings of Studies of Stress Granule Assembly and Composition.Methods in molecular biology (Clifton, N.J.) · 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
- ncRNA BC1 influences translation in the oocyte.RNA biology · 2021Article
- The molecular biology of FMRP: new insights into fragile X syndrome.Nature reviews. Neuroscience · 2021Review
- Dynamics of the fragile X mental retardation protein correlates with cellular and synaptic properties in primary auditory neurons following afferent deprivation.The Journal of comparative neurology · 2021Article
- E-cadherin Interacts With Posttranslationally-Modified AGO2 to Enhance miRISC Activity.Frontiers in cell and developmental biology · 2021Article
- Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation.Frontiers in molecular biosciences · 2021Article
- mTORC1 Crosstalk With Stress Granules in Aging and Age-Related Diseases.Frontiers in aging · 2021Review
- Mammalian stress granules and P bodies at a glance.Journal of cell science · 2020Review
- Regulation of RNA granules by FMRP and implications for neurological diseases.Traffic (Copenhagen, Denmark) · 2020Review
- Cdh1-APC Regulates Protein Synthesis and Stress Granules in Neurons through an FMRP-Dependent Mechanism.iScience · 2020Article
- Canonical nucleators are dispensable for stress granule assembly inJournal of cell science · 2020Article
- RNase L promotes the formation of unique ribonucleoprotein granules distinct from stress granules.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The fragile X mental retardation protein (FMRP) is an RNA-binding protein involved in the mRNA metabolism. The absence of FMRP in neurons leads to alterations of the synaptic plasticity, probably as a result of translation regulation defects. The exact molecular mechanisms by which FMRP plays a role in translation regulation have remained elusive. The finding of an interaction between FMRP and the RNA interference silencing complex (RISC), a master of translation regulation, has suggested that both regulators could be functionally linked. We investigated here this link, and we show that FMRP exhibits little overlap both physically and functionally with the RISC machinery, excluding a direct impact of FMRP on RISC function. Our data indicate that FMRP and RISC are associated to distinct pools of mRNAs. FMRP, unlike RISC machinery, associates with the pool of mRNAs that eventually goes into stress granules upon cellular stress. Furthermore, we show that FMRP plays a positive role in this process as the lack of FMRP or a point mutant causing a severe fragile X alter stress granule formation. Our data support the proposal that FMRP plays a role in controlling the fate of mRNAs after translation arrest.
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Registered trials
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.