Cited by 233Alzheimer's disease research and treatmentsCell death mechanisms and regulationMicrotubule and mitosis dynamics

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Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

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Canu, Nadia, Dus, Laura, Barbato, Christian, Ciotti, Maria T., Brancolini, Claudio, Rinaldi, Anna M., Novak, Michal, Cattaneo, Antonino, Bradbury, Andrew, Calissano, Pietro·1998·The Journal of Neuroscience

DOI 10.1523/jneurosci.18-18-07061.1998PMC PMC6793249

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Abstract

Cerebellar granule cells undergo apoptosis in culture after deprivation of potassium and serum. During this process we found that tau, a neuronal microtubule-associated protein that plays a key role in the maintenance of neuronal architecture, and the pathology of which correlates with intellectual decline in Alzheimer’s disease, is cleaved. The final product of this cleavage is a soluble dephosphorylated tau fragment of 17 kDa that is unable to associate with microtubules and accumulates in the perikarya of dying cells. The appearance of this 17 kDa fragment is inhibited by both caspase and calpain inhibitors, suggesting that tau is an in vivo substrate for both of these proteases during apoptosis. Tau cleavage is correlated with disruption of the microtubule network, and experiments with colchicine and taxol show that this is likely to be a cause and not a consequence of tau cleavage. These data indicate that tau cleavage and change in phosphorylation are important early factors in the failure of the microtubule network that occurs during neuronal apoptosis. Furthermore, this study introduces new insights into the mechanism(s) that generate the truncated forms of tau present in Alzheimer’s disease.

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Authors: Canu, N., Dus, L., Barbato, C., Ciotti, M. T., Brancolini, C., Rinaldi, A. M., Novak, M., Cattaneo, A., Bradbury, A., & Calissano, P.
Affiliations: University of Rome Tor Vergata (IT)
Institute of Neurobiology and Molecular Medicine (IT)
AREA Science Park (IT)
Scuola Internazionale Superiore di Studi Avanzati (IT)
ORCID: Barbato, Christian
Brancolini, Claudio
Rinaldi, Anna M.
Cattaneo, Antonino
Bradbury, Andrew
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 1998-09-15
Volume: 18
Issue: 18
Pages: 7061-7074
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.18-18-07061.1998
PMC: PMC6793249
OpenAlex: W2122437043
Cited by: 232
References: 71
Citations by year: 2026: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 6 · 2019: 6 · 2018: 13 · 2017: 7 · 2016: 3 · 2015: 7 · 2014: 13 · 2013: 9 · 2012: 6
FWCI: 8.40
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 181 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion, other-oa)
Institutional Research Information System (University of Udine) (submittedVersion)
Scuola Normale Superiore di Pisa (submittedVersion)
Funders: Consiglio Nazionale delle Ricerche
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: tau protein, tau cleavage, tau dephosphorylation, cerebellar granule cells, neuronal apoptosis, caspases, calpain, microtubule-associated proteins, Alzheimer's disease
MeSH terms: Alzheimer Disease, Animals, Antineoplastic Agents, Phytogenic, Calpain, Cerebellum, Colchicine, Cysteine Endopeptidases, Cytoskeleton, Enzyme Precursors, Microtubules, Neurons, Oligopeptides, Peptide Fragments, Phosphorylation, Solubility, Cysteine Proteinase Inhibitors, tau Proteins, Rats, Wistar, Apoptosis, Paclitaxel, Caspases, Rats, Caspase 3

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Tau Cleavage and Dephosphorylation in Cerebellar Granule Neurons Undergoing Apoptosis

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