The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo
Open accessAbstract
Emerging studies suggest a role for tau in regulating the biology of RNA binding proteins (RBPs). We now show that reducing the RBP T-cell intracellular antigen 1 (TIA1) in vivo protects against neurodegeneration and prolongs survival in transgenic P301S Tau mice. Biochemical fractionation shows co-enrichment and co-localization of tau oligomers and RBPs in transgenic P301S Tau mice. Reducing TIA1 decreased the number and size of granules co-localizing with stress granule markers. Decreasing TIA1 also inhibited the accumulation of tau oligomers at the expense of increasing neurofibrillary tangles. Despite the increase in neurofibrillary tangles, TIA1 reduction increased neuronal survival and rescued behavioral deficits and lifespan. These data provide in vivo evidence that TIA1 plays a key role in mediating toxicity and further suggest that RBPs direct the pathway of tau aggregation and the resulting neurodegeneration. We propose a model in which dysfunction of the translational stress response leads to tau-mediated pathology.
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“The cell body MAPT pathology is particularly important because this pathology colocalizes with markers of the translational stress response, such as stress granule proteins HNRNPA2B1, TIA1, EIF3n and PABP, and also neuronal death (as shown by cleaved caspase 3 and loss of NeuN positive cells) (Ash et al., 2014; Apicco et al., 2018; Maziuk et al., 2018; Apicco et al., 2019; Jiang et al., 2019, 2021”
From β-amyloid accumulation enhances microtubule associated protein tau pathology in an APPNL-G-F/MAPTP301S mouse model of Alzheimer’s disease (2024) · cites this paper as Apicco et al., 2018
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“Tau-RBP interactions disrupt RNA splicing resulting in gene dysregulation and neurotoxicity (Apicco et al., 2018; Bai et al., 2013; Hsieh et al., 2019).”
From Selective removal of astrocytic APOE4 strongly protects against tau-mediated neurodegeneration and decreases synaptic phagocytosis by microglia (2021) · cites this paper as Apicco et al., 2018
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Cites
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Tau in physiology and pathology
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Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · cited 11×
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InfluentialDecoding ALS: from genes to mechanism
Taylor, J. P., Brown, R. H., & Cleveland, D. W. (2016) · Nature · doi:10.1038/nature20413 · Cited by 2,120 · cited 5×
“This work suggests that the pathophysiology of tauopathy is dependent on the interaction of tau with RBPs, and add tauopathies such as AD and FTD to the growing list of diseases linked to the dysfunction of RNA metabolism.”
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Protein Phase Separation: A New Phase in Cell Biology
Boeynaems, S., Alberti, S., Fawzi, N. L., Mittag, T., Polymenidou, M., Rousseau, F., Schymkowitz, J. W. H., Shorter, J., Wolozin, B. L., Bosch, L. V. D., et al. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.004 · Cited by 2,001
Self-citationBiomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,165
Stress granules and neurodegeneration
Wolozin, B., & Ivanov, P. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 810
Self-citationConverging pathways in neurodegeneration, from genetics to mechanisms
Gan, L., Cookson, M. R., Petrucelli, L., & Spada, A. R. L. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0237-7 · Cited by 500
Stress Granule Assembly Disrupts Nucleocytoplasmic Transport
Zhang, K., Daigle, J. G., Cunningham, K. M., Coyne, A. N., Ruan, K., Grima, J. C., Bowen, K., Wadhwa, H., Yang, P., Rigo, F., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.025 · Cited by 420
“Indeed, loss of SG proteins Ataxin-2 or TIA-1 has been shown to suppress toxicity in yeast and animal models of ALS or tauopathies (Apicco et al., 2018; Elden et al., 2010; Kim et al., 2014).”
Metadata
- Authors
- Apicco, D. J., Ash, P. E. A., Maziuk, B., LeBlang, C., Medalla, M., Al Abdullatif, A., Ferragud, A., Botelho, E., Ballance, H. I., Dhawan, U., Boudeau, S., Cruz, A. L., Kashy, D., Wong, A., Goldberg, L. R., Yazdani, N., Zhang, C., Ung, C. Y., Tripodis, Y., Kanaan, N. M., Ikezu, T., Cottone, P., Leszyk, J., Li, H., Luebke, J., Bryant, C. D., & Wolozin, B.
- Affiliations
- Boston University (US)
- Mayo Clinic (US)
- Michigan State University (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Wolozin, Benjamin
- ORCID
- Apicco, Daniel J.
- Ash, Peter E. A.
- LeBlang, Chelsey
- Medalla, Maria
- Ferragud, Antonio
- Ballance, Heather I.
- Dhawan, Uma
- Cruz, Anna Lourdes
- Kashy, Daniel
- Goldberg, Lisa R.
- Zhang, Cheng
- Ung, Choong Y.
- Tripodis, Yorghos
- Kanaan, Nicholas M.
- Ikezu, Tsuneya
- Cottone, Pietro
- Li, Hu
- Luebke, Jennifer
- Bryant, Camron D.
- Wolozin, Benjamin
- Venue
- Nature Neuroscience
- Published
- 2017-11-20
- Volume
- 21
- Issue
- 1
- Pages
- 72-80
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC5745051
- OpenAlex
- W2768176302
- Cited by
- 281
- References
- 47
- Citations by year
- 2026: 28 · 2025: 35 · 2024: 26 · 2023: 24 · 2022: 42 · 2021: 32 · 2020: 33 · 2019: 34 · 2018: 25 · 2017: 1
- FWCI
- 18.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Glenn Foundation for Medical Research
- National Institutes of Health (1s10od023663-01)
- National Institute on Aging (RF1AG056318, R01AG050471, RF1AG054199, P30AG013846, R01AG054199)
- National Institute of General Medical Sciences (T32GM008541)
- National Institute of Neurological Disorders and Stroke (R01NS089544)
- National Institute of Environmental Health Sciences (R01ES020395)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- TIA-1, RNA-binding proteins, tau protein, tauopathy, neurodegeneration, stress granules, tau oligomers, neurofibrillary tangles, tau aggregation, lifespan, behavioral deficits
- MeSH terms
- Animals, Animals, Newborn, Cognition Disorders, Cytoplasm, Disease Models, Animal, Endoribonucleases, Female, Gene Expression Regulation, Locomotion, Male, Mice, Inbred C57BL, Mice, Transgenic, Mutation, Neurons, Synapses, Trans-Activators, RNA-Binding Proteins, Neurofibrillary Tangles, tau Proteins, Maze Learning, Tauopathies, Mice
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