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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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InfluentialDecoding ALS: from genes to mechanism
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Pathogenic tau inhibits synaptic plasticity by blocking eIF4B-mediated local protein synthesisPreprint
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“The TIA1/Tau interaction induces SG assembly (with long-lived SG), cytotoxic and accelerate neurodegeneration [66,67].”
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Annexin A7 enhances TIA1 axonal trafficking to counteract pathological aggregation in neurons
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Reduced plasma TIA-1: bridging established pathology and novel biomarker potential
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“In line with its central role in stress granule assembly and Tau-related neuroinflammation [6, 22], we hypothesize that plasma TIA-1 may index upstream stress granule/tau-oligomer biology across different disease etiologies.”
InfluentialTrigo-Alonso, P., Luengo, E., Fernández‐Mendívil, C., Viqueira, L., García‐Magro, N., del Sastre, E., Bernal, J. A., Negredo, P., & López, M. G. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02291-1 · Cited by 1
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Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling LawsPreprint
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MARK4 enhances stress granule formation and increases tau accumulationPreprint
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“SGs are heterogenous in their components and properties (15), and SGs containing the RNA binding protein T-cell intracellular antigen 1 (TIA1) have been specifically linked to tau abnormality (16-20).”
Saleem, T., Schmitz, M., Zafar, S., Correia, S., Fernandez, L. C. F., Fischer, A.-L., Thomas, C., Goebel, S., Möbius, W., Younas, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.20.665556 · Cited by 1
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“The S1p fraction were generated as described previously (Apicco et al., 2018).”
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Self-citationFaculty Opinions recommendation of Stress granule assembly disrupts nucleocytoplasmic transport.
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Cytosolic condensates enriched in polyserine repeats are preferred sites of tau fiber propagationPreprint
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Self-citationProteomic and in silico dissection of MetaAggregates in amyotrophic lateral sclerosis brainsPreprint
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Additional file 1 of Altered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Figshare · doi:10.6084/m9.figshare.14812347
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Additional file 3 of Altered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Figshare · doi:10.6084/m9.figshare.14812353
Rispe, C., Hervet, C., de la Cotte, N., Daveu, R., Labadie, K., Noël, B., Aury, J., Thany, S. H., Taillebois, E., Cartereau, A., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20130869
Additional file 2 of Altered ribosomal function and protein synthesis caused by tau
Evans, H. T., Taylor, D. W., Kneynsberg, A., Bodea, L., & Götz, J. (2021) · Figshare · doi:10.6084/m9.figshare.14812350
Rispe, C., Hervet, C., de la Cotte, N., Daveu, R., Labadie, K., Noël, B., Aury, J., Thany, S. H., Taillebois, E., Cartereau, A., et al. (2022) · Figshare · doi:10.6084/m9.figshare.20130890
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“…with the biogenesis or recycling of ribosomes (Evans et al , 2021b), sequester various initiation and elongation factors(Kauwe et al , 2025), and alter the availability of certain mRNAs through its interaction with various RNA-binding proteins (RBPs) (Apicco et al , 2018; Vanderweyde et al , 2016).”
Implications of virus-induced stress granules in tauopathies
Sharma, S., Vandenakker, A., Cortes-Pérez, C. M., Milne, S., & Douville, R. N. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00538-4
“Most studies indicate a relationship between tauopathy and SGs; however, some have reported contradictory findings [103]. eIF3 complex The eIF3 complex is made up of multiple subunits that attaches to the 40S ribosomal subunit and is involved in various stages of the translation initiation process.”
InfluentialLiquid–liquid phase separation of tau in Alzheimer’s disease
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Chronic stress and glucocorticoid actions in brain plasticity and Tau pathology
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RESCUE: recovery of unattributed expression patterns in spatial transcriptomics
Lee, Y. J., Yeo, S. Y., Schrader, A. W., Lee, J., Traniello, I. M., Asadian, M., Ahmed, A. C., Robinson, G. E., Han, H., & Zhao, S. D. (2026) · Nature Communications · doi:10.1038/s41467-026-71720-5
“…that are central to synaptic development and plasticity 26 – 30 and diseases such as amyotrophic lateral sclerosis 31,32 , as well as cytoplasmic transcripts that regulate key processes such as metabolism, signaling, and stress responses 33 – 35 and are involved in Alzheimer ’ s disease 36,37 .”
Hill, E., Linehan, J. M., Farmer, M., Jakubcova, T., Hamdan, S., Tomlinson, A., Purro, S. A., Argentina, F., Jones, E. L., Kaye, N., et al. (2026) · Acta Neuropathologica · doi:10.1007/s00401-026-03009-2
“Furthermore, the observed dissociation between tau burden and toxicity aligns with previous studies showing functional preservation despite persistent pathology [2, 3, 10, 38, 42, 44, 46].”
Fu, Q., Liu, Y., Li, F., Wang, Y., Yue, J., Chen, Y., Wu, S., Zhang, J., Jia, M., He, Y., et al. (2026) · Journal of Neuroinflammation · doi:10.1186/s12974-026-03833-z
“Indeed, previous studies have shown that TIA1 promotes generation of toxic oligomeric tau in primary cultured hippocampal neurons [49], and reducing TIA1 globally in vivo protects against neurodegeneration and prolongs survival in transgenic P301S Tau mice [50].”
Mori, R. D., Ciaiola, F., Nesci, V., Gimenez, J., Bardi, M. D., Pieroni, L., Stefano, S. D., Borsellino, G., Valle, C., Ferri, A., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05885-x
“The interaction of Tau with the SG-nucleating RNA-binding protein (RBP) TIA1 is well established [10], and has been proven necessary for Tau-dependent neurodegeneration in the AD mouse model PS19 [12].”
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Silva-Llanes, I., Baceiredo-Macho, P., & Lastres‐Becker, I. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107454
Kashtiban, B. A., Rezazadeh, M., Gharesouran, J., Jafari, B., & Ghafouri‐Fard, S. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.111974
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Plano, L. M. D., Saitta, A., Minuti, A., Muscarà, C., Gasparo, I., Licitri, L., Sciuto, E. L., Sabrina Conoci, A., Schepici, G., Caccamo, A., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05982-x
“Morphologi-cally, SH-Tau cells exhibited shortened neurites and reduced arborization, confirming previous reports in both in vitro and in vivo models of tauopathy [25, 26].”
Riboregulation: a non-canonical tau function
LeBlanc, K. R., Eck, R. J., Benbow, S. J., & Kraemer, B. C. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00949-x
“Addition of tau accelerates stress granule formation while TIA1 knockdown inhibits tau misfolding and toxicity in cell culture [93] and in P301S Tau mice [109].”
Zhang, M., & Cheng, A. (2026) · Pharmacological Research · doi:10.1016/j.phrs.2026.108312
Gong, Y., Qu, M., Xu, Y., Bao, H., Shen, T., Zeng, L., Wu, X., & He, Q. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102333
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“Moreover, TIA1 haploinsufficiency aggravates neuroinflammatory responses in models of tau-associated neurodegeneration [93,104], further highlighting its relevance in the contexts of disease.”
Tau reduction counteracts transcriptomic and behavioral abnormalities in an Alzheimer amyloid modelPreprint
Knowles, S. J., Sant, C., Nambiar, P., Gonçalves, R. A., Ho, K., Yu, G.-Q., Thomas, R., Mori, M., Domke, L., Huang, V., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.03.741071
Takahashi, M., Abe, T., & Fujii, M. (2026) · Molecular and Cellular Biology · doi:10.1080/10985549.2026.2705871
“98 Interestingly, the heterozygous knockout of Usp10 in mice also extends survival, but only until approximately 49 weeks of age, after which the benefit of the Usp10 knockout is lost.”
Investigating the role of EFhd2 protein in modulating tau pathology in a tauopathy mouse model
Soliman, A. S., Umstead, A., & Vega, I. E. (2026) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2026.1833887
“The sample size for the cross-sectional study (Figure 1) was estimated according to previous experiments and published research (Apicco et al., 2018).”
Chintalapally, S., Rajanala, K., & Upadhyay, A. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1912268
“This bidirectional relationship suggests that elevated TIA1 in AD hippocampus (Acquaah-Mensah et al., 2015) may promote rather than suppress tau pathology (Apicco et al., 2018; Vanderweyde et al., 2016).”
MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation
Nakajima, S., Watanabe, K., Sultanakhmetov, G., Fukuchi, A., Ito, K., Shimizu, S., Saito, T., Asada, A., & Ando, K. (2026) · FEBS Open Bio · doi:10.1002/2211-5463.70338 · Cited by 1
Rougemont, B., Borgel, J., Walker, Z., Zubiri, I., provided, R. O. N., Nafchi, N. A. M., Shaw, C. E., Sirka, E., Isaac, J., Miranda, C. J., et al. (2026) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c01164
TIA1 is required for microglial activation in tauopathy
Webber, C. J., van der Spek, S. J. F., Cruz, A. L., Puri, S., Shao, Y., Zhang, C., Aw, J. T. M., Papadimitriou, G.-Z., Roberts, R., Jiang, K., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118199
Self-citation
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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