On BC1 RNA and the fragile X mental retardation protein
Open accessAbstract
The fragile X mental retardation protein (FMRP), the functional absence of which causes fragile X syndrome, is an RNA-binding protein that has been implicated in the regulation of local protein synthesis at the synapse. The mechanism of FMRP's interaction with its target mRNAs, however, has remained controversial. In one model, it has been proposed that BC1 RNA, a small non-protein-coding RNA that localizes to synaptodendritic domains, operates as a requisite adaptor by specifically binding to both FMRP and, via direct base-pairing, to FMRP target mRNAs. Other models posit that FMRP interacts with its target mRNAs directly, i.e., in a BC1-independent manner. Here five laboratories independently set out to test the BC1-FMRP model. We report that specific BC1-FMRP interactions could be documented neither in vitro nor in vivo. Interactions between BC1 RNA and FMRP target mRNAs were determined to be of a nonspecific nature. Significantly, the association of FMRP with bona fide target mRNAs was independent of the presence of BC1 RNA in vivo. The combined experimental evidence is discordant with a proposed scenario in which BC1 RNA acts as a bridge between FMRP and its target mRNAs and rather supports a model in which BC1 RNA and FMRP are translational repressors that operate independently.
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FMRP's control of Arc is a prime example of its role in mRNA trafficking and expression.
“Its control of Arc is a prime example (Iacoangeli et al., 2008).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Iacoangeli et al., 2008
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- Authors
- Iacoangeli, A., Rozhdestvensky, T. S., Dolzhanskaya, N., Tournier, B., Schütt, J., Brosius, J., Denman, R. B., Khandjian, E. W., Kindler, S., & Tiedge, H.
- Affiliations
- State University of New York (US)
- University of Münster (DE)
- Department of Molecular Biology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314;
- Université Laval (CA)
- University Medical Center Hamburg-Eppendorf (DE)
- Département de Biologie Médicale, Faculté de Médecine, Université Laval, Québec, QC, Canada G1L 3L5; and
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-01-15
- Volume
- 105
- Issue
- 2
- Pages
- 734-739
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2206605
- OpenAlex
- W2002617729
- Cited by
- 83
- References
- 40
- Citations by year
- 2023: 1 · 2021: 4 · 2020: 4 · 2019: 1 · 2018: 4 · 2017: 5 · 2016: 1 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 12
- FWCI
- 7.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS046769, NS046769)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD43428, K12HD043428)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- FMRP, BC1 RNA, fragile X syndrome, RNA-binding proteins, RNA-protein interactions, protein synthesis inhibition, non-coding RNA
- MeSH terms
- Animals, Brain, Gene Expression Regulation, Nucleic Acid Hybridization, RNA, Messenger, Protein Biosynthesis, RNA-Binding Proteins, Mice, Knockout, Biotinylation, RNA, Small Cytoplasmic, Immunoprecipitation, Mice, Fragile X Mental Retardation Protein, Fragile X Messenger Ribonucleoprotein 1
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