Dynamic association with polysomes during P19 neuronal differentiation and an untranslated-region-dependent translation regulation of the tau mRNA by the tau mRNA-associated proteins IMP1, HuD, and G3BP1
Abstract
Regulation of mRNA translation is a key step in mediating neuronal polarity during differentiation, insofar as neuronal polarity is partially determined by local translation of specific mRNA molecules as dendrites and axons are emanating. The multiplicity of mRNA-binding proteins in neurons plays an essential role in controlling mRNA translation. These proteins are associated with ribosomes and translation factors, thereby regulating both temporally and spatially the translation process. In a previous study, we have shown an association among the tau mRNA-binding proteins HuD, IMP1, and G3BP1 with translating polysomes in P19 neurons. In the present study, we determined the dynamics of the association among G3BP1, IMP1, and HuD with polysomes through P19 neuronal differentiation as well as the functional effect of these proteins on tau mRNA translation. We show a novel, differentiation-dependent association of these proteins with polysomes. In addition, we show a strong, negative effect on translation of the tau mRNA by IMP1, G3BP1, and HuD proteins in HEK-293 cells. To our knowledge this is the first observation of a direct translational role of G3BP1 for any mRNA and the first report of a translation inhibition by IMP1 and HuD on the tau mRNA in a cell system. The translation inhibition is shown to be mediated by the tau mRNA 3'untranslated regions (UTRs), thus giving a new, translational role for these sequences, which were previously implicated in mRNA stabilization. We a…
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ELAVL4 binds the 3′ UTR of MAPT RNA in rat primary neurons and in mouse P19 cells.
“ELAVL4 binds the 3′ UTR of MAPT RNA in rat primary neurons and in mouse P19 cells”
From ELAVL4, splicing, and glutamatergic dysfunction precede neuron loss in MAPT mutation cerebral organoids (2021) · cites this paper as Atlas et al., 2007
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References 56 · Cited by 41
- Authors
- Atlas, R., Behar, L., Sapoznik, S., & Ginzburg, I.
- Affiliations
- Weizmann Institute of Science (IL)
- Corresponding author
- Ginzburg, Irith
- Venue
- Journal of Neuroscience Research
- Publisher
- Wiley
- Published
- 2006-11-03
- Volume
- 85
- Issue
- 1
- Pages
- 173-183
- ISSN
- 0360-4012 (ISSN-L)
- 1097-4547
- OpenAlex
- W2054020024
- Cited by
- 41
- References
- 56
- Citations by year
- 2026: 1 · 2022: 3 · 2021: 1 · 2020: 1 · 2019: 3 · 2018: 1 · 2016: 4 · 2015: 3 · 2014: 1 · 2013: 8 · 2012: 6
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Neuroscience Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- mRNA translation regulation, polysomes, IMP-1, HUD, G3BP1, mRNA-binding proteins, 3' untranslated region, neuronal differentiation, P19 cells, protein synthesis inhibition, neuronal polarity
- MeSH terms
- Animals, Cell Differentiation, Humans, Neurons, Polyribosomes, RNA, Messenger, Transfection, Protein Biosynthesis, Neoplastic Stem Cells, Blotting, Northern, RNA-Binding Proteins, tau Proteins, Protein Structure, Tertiary, Untranslated Regions, Cell Line, Tumor, Mice
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