U1 small nuclear ribonucleoproteins (snRNPs) aggregate in Alzheimer’s disease due to autosomal dominant genetic mutations and trisomy 21
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BACKGROUND: We recently identified U1 small nuclear ribonucleoprotein (snRNP) tangle-like aggregates and RNA splicing abnormalities in sporadic Alzheimer's disease (AD). However little is known about snRNP biology in early onset AD due to autosomal dominant genetic mutations or trisomy 21 in Down syndrome. Therefore we investigated snRNP biochemical and pathologic features in these disorders. FINDINGS: We performed quantitative proteomics and immunohistochemistry in postmortem brain from genetic AD cases. Electron microscopy was used to characterize ultrastructural features of pathologic aggregates. U1-70k and other snRNPs were biochemically enriched in the insoluble fraction of human brain from subjects with presenilin 1 (PS1) mutations. Aggregates of U1 snRNP-immunoreactivity formed cytoplasmic tangle-like structures in cortex of AD subjects with PS1 and amyloid precursor protein (APP) mutations as well as trisomy 21. Ultrastructural analysis with electron microscopy in an APP mutation case demonstrated snRNP immunogold labeling of paired helical filaments (PHF). CONCLUSIONS: These studies identify U1 snRNP pathologic changes in brain of early onset genetic forms of AD. Since dominant genetic mutations and trisomy 21 result in dysfunctional amyloid processing, the findings suggest that aberrant β-amyloid processing may influence U1 snRNP aggregate formation.
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U1 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 [136]
Many U1 snRNPs colocalize with neurofibrillary tangles and paired helical filaments in AD brain.
“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 [34]
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 [34]
U1 snRNPs are a major component of the AD insoluble proteome.
“We have previously shown that U1 snRNPs are a major component of the AD insoluble proteome [24, 32–34].”
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 [34]
U1 spliceosome proteins undergo a dramatic shift in solubility in AD brain and aggregate in close proximity to neurofibrillary tangles.
“This may be due to the fact that U1 spliceosome proteins undergo a dramatic shift in solubility in AD brain, and aggregate in close proximity to neurofibrillary tangles [24, 32–34].”
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 [34]
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Bai, B., Vanderwall, D., Li, Y., Wang, X., Poudel, S., Wang, H., Dey, K. K., Chen, P., Yang, K., & Peng, J. (2021) · Figshare · doi:10.6084/m9.figshare.15162179
Ai, R., Mao, L., Jin, X., Zhang, S., Pan, J., Lagartos-Donate, M. J., Cao, S., Yang, G., Xie, C., Kang, X., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.27.620478
Roles of RNA-Binding Nuclear Proteins in Alzheimer’s Disease Pathophysiology
Kumar, S., & Upadhyay, A. (2026) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.6c00028
Aβ Aggregates Bind the U1 Spliceosomal Ribonucleoprotein in Alzheimer Disease BrainPreprint
Tao, Y., Francis, A. E., Liu, W., Watkins, C., Bennett, D. A., Selkoe, D. J., Flynn, R. A., & Stern, A. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.02.729610
Peng, B., Zou, S., Shi, Y., Zhu, X., Liu, M., Li, H., & Zhang, Y. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153818
Contribution of G4 Structure to Alzheimer’s Disease and Tau Pathology
Kallweit, L. M. (2026) · doi:10.56902/etdcrp.2026.63
- Authors
- Hales, C. M., Seyfried, N. T., Dammer, E. B., Duong, D., Yi, H., Gearing, M., Troncoso, J. C., Mufson, E. J., Thambisetty, M., Levey, A. I., & Lah, J. J.
- Affiliations
- Emory University (US)
- Johns Hopkins University (US)
- Rush University (US)
- National Institutes of Health (US)
- Corresponding author
- Lah, James J
- ORCID
- Venue
- Molecular Neurodegeneration
- Published
- 2014-04-28
- Volume
- 9
- Issue
- 1
- Pages
- 15-15
- ISSN
- 1750-1326 (ISSN-L)
- PMC
- PMC4022210
- OpenAlex
- W2143216632
- Cited by
- 58
- References
- 28
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 6 · 2020: 5 · 2019: 2 · 2018: 10 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 1
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Neurodegeneration (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association (NIRG-12-242297)
- American Brain Foundation
- Emory University (AG025688, P30NS055077)
- University of Washington
- National Institutes of Health (AG05136, AG025688)
- Alzheimer's Disease Research Center, Emory University (AG025688, AG05136)
- National Institute on Aging (P50 AG05136, AG 05136, AG 025688, P01AG014449, P01 AG14449, R01AG043375, P50AG005136, P50AG025688)
- National Institute of Neurological Disorders and Stroke (P30NS055077)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- U1 snRNA, small nuclear ribonucleoproteins, Alzheimer's disease, Down syndrome, presenilin 1 mutations, amyloid precursor protein mutations, RNA splicing, protein aggregation, paired helical filaments
- MeSH terms
- Adult, Aged, Aged, 80 and over, Alzheimer Disease, Down Syndrome, Female, Humans, Immunohistochemistry, Male, Middle Aged, Mutation, Amyloid beta-Protein Precursor, Ribonucleoprotein, U1 Small Nuclear, Microscopy, Electron, Transmission, Presenilin-1
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