ArticleMolecular and cellular biology2002
Casein kinase II phosphorylates the fragile X mental retardation protein and modulates its biological properties.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 85 citations in OpenAlex.
- FMRP drives mRNP targets into translationally silenced complexes.Molecular cell · 2025Article
- Increased degradation of FMRP contributes to neuronal hyperexcitability in tuberous sclerosis complex.Cell reports · 2023Article
- Diverse roles of biomolecular condensation in eukaryotic translational regulation.RNA biology · 2023Review
- Hamster PIWI proteins bind to piRNAs with stage-specific size variations during oocyte maturation.Nucleic acids research · 2021Article
- Fragile X-related protein family: a double-edged sword in neurodevelopmental disorders and cancer.Critical reviews in biochemistry and molecular biology · 2020Review
- Post-translational modifications of the Fragile X Mental Retardation Protein in neuronal function and dysfunction.Molecular psychiatry · 2020Review
- Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Expression and Characterization of Human Fragile X Mental Retardation Protein Isoforms and Interacting Proteins in Human Cells.Proteomics insights · 2019Article
- Unraveling the Pathways to Neuronal Homeostasis and Disease: Mechanistic Insights into the Role of RNA-Binding Proteins and Associated Factors.International journal of molecular sciences · 2018Review
- Altered expression of the FMR1 splicing variants landscape in premutation carriers.Biochimica et biophysica acta. Gene regulatory mechanisms · 2017Article
- Drosophila Protein Kinase CK2: Genetics, Regulatory Complexity and Emerging Roles during Development.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Fragile X mental retardation protein: A paradigm for translational control by RNA-binding proteins.Biochimie · 2015Review
- Comparison of Equivalence between Two Commercially Available S499-Phosphorylated FMRP Antibodies in Mice.PloS one · 2015Article
- Fragile X mental retardation protein regulates translation by binding directly to the ribosome.Molecular cell · 2014Article
- Article
- Biophysical characterization of G-quadruplex forming FMR1 mRNA and of its interactions with different fragile X mental retardation protein isoforms.RNA (New York, N.Y.) · 2014Article
- FMRP regulates actin filament organization via the armadillo protein p0071.RNA (New York, N.Y.) · 2013Article
- Characterization of Fragile X Mental Retardation Protein granules formation and dynamics in Drosophila.Biology open · 2013Article
- Characterization of fragile X mental retardation protein recruitment and dynamics in Drosophila stress granules.PloS one · 2013Article
- FMR1 transcript isoforms: association with polyribosomes; regional and developmental expression in mouse brain.PloS one · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fragile X syndrome is caused by loss of FMR1 protein expression. FMR1 binds RNA and associates with polysomes in the cytoplasm; thus, it has been proposed to function as a regulator of gene expression at the posttranscriptional level. Posttranslational modification of FMR1 had previously been suggested to regulate its activity, but no experimental support for this model has been reported to date. Here we report that FMR1 in Drosophila melanogaster (dFMR1) is phosphorylated in vivo and that the homomer formation and the RNA-binding activities of dFMR1 are modulated by phosphorylation in vitro. Identification of a protein phosphorylating dFMR1 showed it to be Drosophila casein kinase II (dCKII). dCKII directly interacts with and phosphorylates dFMR1 in vitro. The phosphorylation site in dFMR1 was identified as Ser406, which is highly conserved among FMR1 family members from several species. Using mass spectrometry, we established that Ser406 of dFMR1 is indeed phosphorylated in vivo. Furthermore, human FMR1 (hFMR1) is also phosphorylated in vivo, and alteration of the conserved Ser500 in hFMR1 abolishes phosphorylation by CKII in vitro. These studies support the model that the biological functions of FMR1, such as regulation of gene expression, are likely regulated by its phosphorylation.
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