ArticleThe Biochemical journal1999
Oligomerization properties of fragile-X mental-retardation protein (FMRP) and the fragile-X-related proteins FXR1P and FXR2P.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 83 citations in OpenAlex.
- The disease-associated proteins Drosophila Nab2 and Ataxin-2 interact with shared RNAs and coregulate neuronal morphology.Genetics · 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
- Absence of RNA-binding protein FXR2P prevents prolonged phase of kainate-induced seizures.EMBO reports · 2021Article
- miR-132 Regulates PTSD-like Behaviors in Rats Following Single-Prolonged Stress Through Fragile X-Related Protein 1.Cellular and molecular neurobiology · 2021Article
- Post-translational modifications of the Fragile X Mental Retardation Protein in neuronal function and dysfunction.Molecular psychiatry · 2020Review
- Expression and Characterization of Human Fragile X Mental Retardation Protein Isoforms and Interacting Proteins in Human Cells.Proteomics insights · 2019Article
- Regulation of Adult Neurogenesis by the Fragile X Family of RNA Binding Proteins.Brain plasticity (Amsterdam, Netherlands) · 2018Review
- Fragile X granules are a family of axonal ribonucleoprotein particles with circuit-dependent protein composition and mRNA cargos.The Journal of comparative neurology · 2018Article
- Hypervariable Domain of Eastern Equine Encephalitis Virus nsP3 Redundantly Utilizes Multiple Cellular Proteins for Replication Complex Assembly.Journal of virology · 2017Article
- Fragile X related protein 1 (FXR1P) regulates proliferation of adult neural stem cells.Human molecular genetics · 2017Article
- Interactions of Alphavirus nsP3 Protein with Host Proteins.Frontiers in microbiology · 2017Review
- Sub-synaptic, multiplexed analysis of proteins reveals Fragile X related protein 2 is mislocalized ineLife · 2016Article
- CMP‑N‑acetylneuraminic acid synthetase interacts with fragile X related protein 1.Molecular medicine reports · 2016Article
- New World and Old World Alphaviruses Have Evolved to Exploit Different Components of Stress Granules, FXR and G3BP Proteins, for Assembly of Viral Replication Complexes.PLoS pathogens · 2016Article
- Fmr1 KO and fenobam treatment differentially impact distinct synapse populations of mouse neocortex.Neuron · 2014Article
- Article
- The FMRP regulon: from targets to disease convergence.Frontiers in neuroscience · 2013Review
- The TSC1-TSC2 complex consists of multiple TSC1 and TSC2 subunits.BMC biochemistry · 2012Article
- Mechanism of repeat-associated microRNAs in fragile X syndrome.Neural plasticity · 2012Review
- The fragile x mental retardation syndrome 20 years after the FMR1 gene discovery: an expanding universe of knowledge.The Clinical biochemist. Reviews · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The absence of fragile-X mental-retardation protein (FMRP) results in fragile-X syndrome. Two other fragile-X-related (FXR) proteins have been described, FXR1P and FXR2P, which are both very similar in amino acid sequence to FMRP. Interaction between the three proteins as well as with themselves has been demonstrated. The FXR proteins are believed to play a role in RNA metabolism. To characterize a possible functional role of the interacting proteins the complex formation of the FXR proteins was studied in mammalian cells. Double immunofluorescence analysis in COS cells over-expressing either FMRP ISO12/FXR1P or FMRP ISO12/FXR2P confirmed heterotypic interactions. However, Western-blotting studies on cellular homogenates containing physiological amounts of the three proteins gave different indications. Gel-filtration experiments under physiological as well as EDTA conditions showed that the FXR proteins were in complexes of >600 kDa, as parts of messenger ribonuclear protein (mRNP) particles associated with polyribosomes. Salt treatment shifted FMRP, FXR1P and FXR2P into distinct intermediate complexes, with molecular masses between 200 and 300 kDa. Immunoprecipitations of FMRP as well as FXR1P from the dissociated complexes revealed that the vast majority of the FXR proteins do not form heteromeric complexes. Further analysis by [(35)S]methionine labelling in vivo followed by immunoprecipitation indicated that no proteins other than the FXR proteins were present in these complexes. These results suggest that the FXR proteins form homo-multimers preferentially under physiological conditions in mammalian cells, and might participate in mRNP particles with separate functions.
Indexed as
Identifiers
10527928PMC1220581W2127453064What OpenQuestion holds
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.