The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
Abstract
We have investigated ubiquitinated paired helical filaments, which produce a proteinaceous smear in SDS-polyacrylamide gel electrophoresis and immunoblotting. The smear consisted largely of the carboxy-terminal portion of tau and ubiquitin. The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. Most ubiquitin in paired helical filaments occurred as a monoubiquitinated form, and only a small proportion of ubiquitin formed multiubiquitin chains. There was a ubiquitin-negative smear, in which tau was much less processed in the amino-terminal portion. This strongly suggests that the amino-terminal processing of tau in paired helical filaments precedes its ubiquitination.
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“Accumulation of ubiquitin-conjugated tau at Lys254, 257, 290, 311, 317 and 353 has been identified in PHF from AD brain and in an AD mouse model [161, 163, 164].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [163]
In the citing paper
“Therefore, ubiquitination plays an important role in maintaining a pool of cellular tau under physiological conditions.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [163]
Citations
Cites
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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
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THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION
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A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
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Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease
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Research works printed but not linked: 1
- DeCarli, 1992, Post-mortem regional neurofibrillary tangle densities but not senile plaque densities are related to regional cerebral metabolic rates for glucose during life in Alzheimer's disease patients, Neurodegeneration, 1, 113
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142
Tau in Alzheimer Disease and Related Tauopathies
Iqbal, K., Liu, F., Gong, C., & Grundke, I. (2010) · Current Alzheimer Research · doi:10.2174/156720510793611592 · Cited by 1,163
Role of tau protein in both physiological and pathological conditions
AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
Metadata
- Authors
- Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y.
- Affiliations
- The University of Tokyo (JP)
- RIKEN (JP)
- Fujita Health University (JP)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 10
- Issue
- 6
- Pages
- 1151-1160
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2012781495
- Cited by
- 332
- References
- 45
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 6 · 2023: 9 · 2022: 9 · 2021: 10 · 2020: 14 · 2019: 9 · 2018: 8 · 2017: 7 · 2016: 13 · 2015: 9 · 2014: 10 · 2013: 3 · 2012: 10
- FWCI
- 10.43
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health and Welfare
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Keywords
- ubiquitin, tau protein, paired helical filaments, ubiquitination, microtubule-binding region, protein aggregation, Alzheimer's disease, ubiquitin chains, post-translational modification
- MeSH terms
- Amino Acid Sequence, Antibodies, Monoclonal, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Humans, Microtubules, Molecular Sequence Data, Molecular Weight, Peptide Fragments, Peptide Mapping, Endopeptidases, Protein Binding, Mass Spectrometry, Ubiquitins, Neurofibrillary Tangles, tau Proteins
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