Cited by 723Alzheimer's disease research and treatmentsHeat shock proteins researchUbiquitin and proteasome pathways

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CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L.·2004·Human Molecular Genetics

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Abstract

Molecular chaperones, ubiquitin ligases and proteasome impairment have been implicated in several neurodegenerative diseases, including Alzheimer's and Parkinson's disease, which are characterized by accumulation of abnormal protein aggregates (e.g. tau and alpha-synuclein respectively). Here we report that CHIP, an ubiquitin ligase that interacts directly with Hsp70/90, induces ubiquitination of the microtubule associated protein, tau. CHIP also increases tau aggregation. Consistent with this observation, diverse of tau lesions in human postmortem tissue were found to be immunopositive for CHIP. Conversely, induction of Hsp70 through treatment with either geldanamycin or heat shock factor 1 leads to a decrease in tau steady-state levels and a selective reduction in detergent insoluble tau. Furthermore, 30-month-old mice overexpressing inducible Hsp70 show a significant reduction in tau levels. Together these data demonstrate that the Hsp70/CHIP chaperone system plays an important role in the regulation of tau turnover and the selective elimination of abnormal tau species. Hsp70/CHIP may therefore play an important role in the pathogenesis of tauopathies and also represents a potential therapeutic target.

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Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
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Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474
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Dikshit, P., & Jana, N. R. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9459-x · Cited by 4
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Nakamura, M., Ito, H., Nakamura, Y., Wate, R., Kaneko, S., Nakano, S., Matsumoto, S.-I., & Kusaka, H. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01120.x · Cited by 4
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Li, X., He, Z., Wang, C., Liu, Y., Shan, Z., Zhang, L., Shi, Q., Yue, C., Lin, Y., Liu, Y., et al. (2020) · Natural Product Communications · doi:10.1177/1934578x20948986 · Cited by 4
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Tian, T. M., McLean, J. W., Wilson, J. A., & Wilson, S. M. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15180 · Cited by 4
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Chi, H., Sang, T., & Chang, H.-Y. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.73198 · Cited by 5
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Pandey, M., Nabi, J., Tabassum, N., Pottoo, F. H., Khatik, R., & Ahmad, N. (2020) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-1317-0.ch014 · Cited by 4
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HSP70 interacting protein prevents the accumulation of inclusions in polyglutamine disease1
Howarth, J. L., Glover, C. P. J., & Uney, J. B. (2009) · Journal of Neurochemistry · doi:10.1111/j.0022-3042.2008.05847.x · Cited by 3
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Tashiro, E., Kitagawa, M., & Imoto, M. (2017) · Springer eBooks · doi:10.1007/978-4-431-56529-1_4 · Cited by 3
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Self-citation
Ubiquitin-Proteasome System Dysregulation in Alzheimer’s Disease Impacts Protein AbundancePreprint
Collins, M. A., Friedrich, C., Elcheikhali, M., Stewart, P., Derks, J., Connors, T. R., Altig, K., Melloni, A. N., Petelski, A. A., Oakley, D. H., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.29.656728 · Cited by 5
Chapter 7 Ubiquitinopathies
Dickson, D. W. (2007) · Blue Books of Neurology · doi:10.1016/s1877-184x(09)70058-9 · Cited by 3
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Chinnathambi, S., & Rangappa, N. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.02.001 · Cited by 4

Authors: Petrucelli, L.
Affiliations: Mayo Clinic in Florida (US)
Corresponding author: Petrucelli, L.
ORCID: Petrucelli, L.
Venue: Human Molecular Genetics
Publisher: Oxford University Press (OUP)
Published: 2004-01-28
Volume: 13
Issue: 7
Pages: 703-714
ISSN: 0964-6906 (ISSN-L)
1460-2083
DOI: 10.1093/hmg/ddh083
OpenAlex: W2168079270
Cited by: 723
References: 41
Citations by year: 2026: 29 · 2025: 36 · 2024: 32 · 2023: 32 · 2022: 37 · 2021: 37 · 2020: 36 · 2019: 25 · 2018: 35 · 2017: 31 · 2016: 31 · 2015: 38 · 2014: 34 · 2013: 28 · 2012: 31
FWCI: 10.76
Type: journal article
Language: en
Open access: closed
Locations: Human Molecular Genetics (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: National Institute of Neurological Disorders and Stroke (R01NS041816, R01-NS41816-01)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: CHIP, HSP70, tau protein, ubiquitination, protein degradation, tau aggregation, molecular chaperones, ubiquitin ligase, geldanamycin, heat shock factor 1, tauopathy, Alzheimer's disease, Parkinson's disease, proteasome
MeSH terms: Heat Shock Transcription Factors, Animals, Cell Line, Detergents, DNA-Binding Proteins, Genetic Vectors, Humans, Immunohistochemistry, Lac Operon, Models, Genetic, Mutation, Nuclear Proteins, Protein Binding, Quinones, Subcellular Fractions, Transcription Factors, Transfection, Blotting, Western, Benzoquinones, tau Proteins, Molecular Chaperones, HSP70 Heat-Shock Proteins, Transgenes, COS Cells, Ubiquitin, Drosophila Proteins, Ubiquitin-Protein Ligases, Cell Line, Tumor, Lactams, Macrocyclic, Immunoprecipitation, Mice

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CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

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