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Kissing complex RNAs mediate interaction between the Fragile-X mental retardation protein KH2 domain and brain polyribosomes
Open accessAbstract
Fragile-X mental retardation is caused by loss of function of a single gene encoding the Fragile-X mental retardation protein, FMRP, an RNA-binding protein that harbors two KH-type and one RGG-type RNA-binding domains. Previous studies identified intramolecular G-quartet RNAs as high-affinity targets for the RGG box, but the relationship of RNA binding to FMRP function and mental retardation remains unclear. One severely affected patient harbors a missense mutation (I304N) within the second KH domain (KH2), and some evidence suggests this domain may be involved in the proposed role of FMRP in translational regulation. We now identify the RNA target for the KH2 domain as a sequence-specific element within a complex tertiary structure termed the FMRP kissing complex. We demonstrate that the association of FMRP with brain polyribosomes is abrogated by competition with the FMRP kissing complex RNA, but not by high-affinity G-quartet RNAs. We conclude that mental retardation associated with the I304N mutation, and likely the Fragile-X syndrome more generally, may relate to a crucial role for RNAs harboring the kissing complex motif as targets for FMRP translational regulation.
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“FMRP also binds to kissing complex sites [18], but APP mRNA lacks such a site.”
From FMRP Mediates mGluR5-Dependent Translation of Amyloid Precursor Protein (2007) · cites this paper as [18]
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Metadata
- Authors
- Darnell, J. C., Fraser, C. E., Mostovetsky, O., Stefani, G., Jones, T. A., Eddy, S. R., & Darnell, R. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2005-04-01
- Volume
- 19
- Issue
- 8
- Pages
- 903-918
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1080130
- OpenAlex
- W2124859239
- Cited by
- 287
- References
- 80
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 6 · 2023: 4 · 2022: 7 · 2021: 10 · 2020: 14 · 2019: 15 · 2018: 13 · 2017: 8 · 2016: 10 · 2015: 12 · 2014: 14 · 2013: 23 · 2012: 19
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (Università degli Studi di Trento) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Memorial Sloan-Kettering Cancer Center
- Weill Cornell Medical College
- National Human Genome Research Institute (R01HG001363, R01-HG01363)
- National Institute of General Medical Sciences (GM 07739, T32GM007739)
- National Institute of Neurological Disorders and Stroke (R01NS040955, R01 NS34389, R01NS034389, NS40955)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01 HD40647, R01HD040647)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- FMRP, polysomes, RNA-binding proteins, translational regulation, RGG domain, fragile X syndrome, RNA tertiary structure, RNA-protein interactions
- MeSH terms
- Animals, Base Sequence, Cerebral Cortex, DNA Mutational Analysis, Fragile X Syndrome, Gene Expression Regulation, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Polyribosomes, RNA, Blotting, Western, RNA-Binding Proteins, Sequence Analysis, DNA, Protein Structure, Tertiary, DNA Primers, Base Pairing, Mutation, Missense, Amino Acid Motifs, Electrophoretic Mobility Shift Assay, Mice, Fragile X Mental Retardation Protein, Fragile X Messenger Ribonucleoprotein 1
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