RNA binding proteins co-localize with small tau inclusions in tauopathy
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The development of insoluble, intracellular neurofibrillary tangles composed of the microtubule-associated protein tau is a defining feature of tauopathies, including Alzheimer's disease (AD). Accumulating evidence suggests that tau pathology co-localizes with RNA binding proteins (RBPs) that are known markers for stress granules (SGs). Here we used proteomics to determine how the network of tau binding proteins changes with disease in the rTg4510 mouse, and then followed up with immunohistochemistry to identify RNA binding proteins that co-localize with tau pathology. The tau interactome networks revealed striking disease-related changes in interactions between tau and a multiple RBPs, and biochemical fractionation studies demonstrated that many of these proteins including hnRNPA0, EWSR1, PABP and RPL7 form insoluble aggregates as tau pathology develops. Immunohistochemical analysis of mouse and human brain tissues suggest a model of evolving pathological interaction, in which RBPs co-localize with pathological phospho-tau but occur adjacent to larger pathological tau inclusions. We suggest a model in which tau initially interacts with RBPs in small complexes, but evolves into isolated aggregated inclusions as tau pathology matures.
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Cell body MAPT pathology colocalizes with markers of the translational stress response, such as stress granule proteins HNRNPA2B1, TIA1, EIF3n and PABP, and also neuronal death (cleaved caspase 3 and loss of NeuN positive cells).
“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 Maziuk et al., 2018
The Results (Figs. 1 and 4; page not provided) show that TIA1 and PABP colocalize with diffuse phosphorylated tau in neuronal cell bodies, but that colocalization is reduced or absent in mature tangles. The proteins reported in Fig. 4 are HNRNPA0 and eIF2α, not the claim’s HNRNPA2B1 and EIF3n. These passages do not establish neuronal death through cleaved caspase 3 or loss of NeuN-positive cells. (LLM, conf=0.88)
Experimental — accuracy not yet measuredU1 small nuclear ribonucleoproteins and other RNA-binding proteins are associated with tau tangles in the AD brain detergent-insoluble proteome.
“previous analyses of the AD brain detergent-insoluble proteome, which have repeatedly demonstrated the association of U1 small nuclear ribonucleoproteins (U1 snRNPs) and other RNA-binding proteins with tau tangles [133–137].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [137]
Accumulation of insoluble snRNPs correlates strongly with both amyloid and Tau pathology.
“Interestingly, our previous studies demonstrated that many of the U1 snRNPs colocalize with neurofibrillary tangles and paired helical filaments in AD brain [24, 32–34], and that accumulation of insoluble snRNPs correlates strongly with both amyloid and Tau pathology [32–37].”
From Deep proteomic network analysis of Alzheimer’s disease brain reveals alterations in RNA binding proteins and RNA splicing associated with disease (2018) · cites this paper as [36]
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Stress granules: emerging players in neurodegenerative diseases
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Increased G3BP2-Tau interaction in tauopathies is a natural defense against Tau aggregation
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Nuclear face of Tau: an inside player in neurodegeneration
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Cellular Biology of Tau Diversity and Pathogenic Conformers
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- Authors
- Maziuk, B. F., Apicco, D. J., Cruz, A. L., Jiang, L., Ash, P. E. A., da Rocha, E. L., Zhang, C., Yu, W. H., Leszyk, J., Abisambra, J. F., Li, H., & Wolozin, B.
- Affiliations
- Boston University (US)
- Mayo Clinic (US)
- Columbia University Irving Medical Center (US)
- University of Massachusetts Chan Medical School (US)
- University of Kentucky (US)
- Corresponding author
- Wolozin, Benjamin
- ORCID
- Venue
- Acta Neuropathologica Communications
- Published
- 2018-08-01
- Volume
- 6
- Issue
- 1
- Pages
- 71-71
- ISSN
- 2051-5960 (ISSN-L)
- PMC
- PMC6069705
- OpenAlex
- W2887193453
- Cited by
- 151
- References
- 45
- Citations by year
- 2026: 18 · 2025: 17 · 2024: 14 · 2023: 20 · 2022: 18 · 2021: 17 · 2020: 25 · 2019: 17 · 2018: 5
- FWCI
- 10.98
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Acta Neuropathologica Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion, cc-by)
- UKnowledge (University of Kentucky) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute on Aging (AG050471, AG056318, AG028383)
- National Institute of Neurological Disorders and Stroke (NS089544, NS106751, NS091329)
- National Institute of Environmental Health Sciences (ES020395)
- BrightFocus Foundation
- Alzheimer Association
- Cure Alzheimer's Fund
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (MD009205)
- U.S. Department of Defense (AZ140097)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tauopathy, tau protein, RNA-binding proteins, stress granules, neurofibrillary tangles, EWSR1, poly(A)-binding protein, protein aggregation, phosphorylated tau, Alzheimer's disease, protein colocalization
- MeSH terms
- T-Cell Intracellular Antigen-1, Aged, Aged, 80 and over, Animals, Brain, Inclusion Bodies, Endodeoxyribonucleases, Humans, Male, Mice, Transgenic, Middle Aged, Phosphorylation, Mass Spectrometry, RNA-Binding Proteins, Neurofibrillary Tangles, tau Proteins, Cell Cycle Proteins, Tauopathies, Proteomics, Immunoprecipitation, Mice, Protein Interaction Maps, Protein Aggregation, Pathological
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