Fragile X mental retardation protein is necessary for neurotransmitter-activated protein translation at synapses
Open accessAbstract
Fragile X mental retardation is caused by absence of the RNA-binding protein fragile X mental retardation protein (FMRP), encoded by the FMR1 gene. There is increasing evidence that FMRP regulates transport and modulates translation of some mRNAs. We studied neurotransmitter-activated synaptic protein synthesis in fmr1 -knockout mice. Synaptoneurosomes from knockout mice did not manifest accelerated polyribosome assembly or protein synthesis as it occurs in wild-type mice upon stimulation of group I metabotropic glutamate receptors. Direct activation of protein kinase C did not compensate in the knockout mouse, indicating that the FMRP-dependent step is further along the signaling pathway. Visual cortices of young knockout mice exhibited a lower proportion of dendritic spine synapses containing polyribosomes than did the cortices of wild-type mice, corroborating this finding in vivo . This deficit in rapid neurotransmitter-controlled local translation of specific proteins may contribute to morphological and functional abnormalities observed in patients with fragile X syndrome.
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DHPG does not increase overall protein synthesis in synaptoneurosomes.
“However, we did not observe an increase in overall protein synthesis in response to DHPG, whereas Weiler and colleagues [31] observed a 1.3-fold increase in 35S-Met incorporation after 5 min of stimulation.”
From FMRP Mediates mGluR5-Dependent Translation of Amyloid Precursor Protein (2007) · cites this paper as [31]
The citation is attached to the statement that Weiler and colleagues observed a 1.3-fold increase in 35S-Met incorporation after five minutes; the preceding statement that no increase was observed is the citing authors’ own result. The available indexed passages have no results section or page text reporting DHPG stimulation or incorporation, and searches for those terms and the 1.3-fold figure found no relevant passage. (LLM, conf=0.72)
Experimental — accuracy not yet measuredFMRP is not required for basal protein synthesis.
“Therefore, FMRP was not required for basal protein synthesis, which is in agreement with a prior report [31].”
From FMRP Mediates mGluR5-Dependent Translation of Amyloid Precursor Protein (2007) · cites this paper as [31]
The passages available from our copy are bibliographic material, including the title, which concerns neurotransmitter-activated translation at synapses. Searches for basal, unstimulated, and baseline protein synthesis found no passage addressing whether FMRP is required for basal synthesis. (LLM, conf=0.70)
Experimental — accuracy not yet measured
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Self-citation
- Authors
- Weiler, I. J., Spangler, C. C., Klintsova, A. Y., Grossman, A. W., Kim, S. H., Bertaina-Anglade, V., Khaliq, H., de Vries, F. E., Lambers, F. A. E., Hatia, F., Base, C. K., & Greenough, W. T.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Beckman Institute, Neuroscience Program, and Departments of Psychology, Psychiatry, and Cell and Structural Biology, University of Illinois at Urbana–Champaign, Urbana, IL 61801
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-11-17
- Volume
- 101
- Issue
- 50
- Pages
- 17504-17509
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC536018
- OpenAlex
- W2007532395
- Cited by
- 210
- References
- 52
- Citations by year
- 2025: 1 · 2024: 3 · 2023: 3 · 2022: 7 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 8 · 2016: 4 · 2015: 10 · 2014: 7 · 2013: 7 · 2012: 16
- FWCI
- 11.25
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- FRAXA Research Foundation (MH35321)
- Universiteit Antwerpen
- National Institutes of Health (5r03hd035565-02, 5r01hd037175-03)
- National Institute of Mental Health (MH-35321, R01MH035321, R37MH035321)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R03 HD 35565-01, HD 37175)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- FMRP, fragile X syndrome, FMR1 gene, synaptic protein synthesis, local translation, group I metabotropic glutamate receptors, protein kinase C, dendritic spines, synaptoneurosomes, visual cortex, Fmr1 knockout mice, RNA-binding proteins
- MeSH terms
- Animals, Glycine, Methionine, Microscopy, Electron, Nerve Tissue Proteins, Potassium, Resorcinols, Ribosomes, Synapses, Protein Biosynthesis, RNA-Binding Proteins, Gene Deletion, Mice, Knockout, Neurotransmitter Agents, Mice, Fragile X Messenger Ribonucleoprotein 1, Fragile X Mental Retardation Protein
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