Cited by 333Alzheimer's disease research and treatmentsUbiquitin and proteasome pathwaysParkinson's Disease Mechanisms and Treatments

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Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

Morishima-Kawashima, Maho, Hasegawa, Masato, Takio, Koji, Suzuki, Masami, Titani, Koiti, Ihara, Yasuo·1993·Neuron

DOI 10.1016/0896-6273(93)90063-w

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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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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)
ORCID: Hasegawa, Masato
Ihara, Yasuo
Venue: Neuron
Publisher: Elsevier BV
Published: 1993-06
Volume: 10
Issue: 6
Pages: 1151-1160
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(93)90063-w
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
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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Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

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