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Differential effect of three‐repeat and four‐repeat tau on mitochondrial axonal transport
Open accessAbstract
Tau protein is present in six different splice forms in the human brain and interacts with microtubules via either 3 or 4 microtubule binding repeats. An increased ratio of 3 repeat to 4 repeat isoforms is associated with neurodegeneration in inherited forms of frontotemporal dementia. Tau over‐expression diminishes axonal transport in several systems, but differential effects of 3 repeat and 4 repeat isoforms have not been studied. We examined the effects of tau on mitochondrial transport and found that both 3 repeat and 4 repeat tau change normal mitochondrial distribution within the cell body and reduce mitochondrial localization to axons; 4 repeat tau has a greater effect than 3 repeat tau. Further, we observed that the 3 repeat and 4 repeat tau cause different alterations in retrograde and anterograde transport dynamics with 3 repeat tau having a slightly stronger effect on axon transport dynamics. Our results indicate that tau‐induced changes in axonal transport may be an underlying theme in neurodegenerative diseases associated with isoform specific changes in tau’s interaction with microtubules.
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Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways have been implicated as consequences of tau mislocalization or oligomerization.
“Mitochondrial abnormalities, synaptic loss and dysfunction, altered axonal transport, and activation of cell death pathways (including caspase activation and inflammatory responses) have all been directly or indirectly implicated as consequences of tau mislocalization or oligomerization (20, 40, 43–52).”
From All the Tau We Cannot See (2023) · cites this paper as [40]
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Metadata
- Authors
- Stoothoff, W., Jones, P. B., Spires‐Jones, T. L., Joyner, D., Chhabra, E., Bercury, K., Fan, Z., Xie, H., Bacskai, B., Edd, J., Irimia, D., & Hyman, B. T.
- Affiliations
- Harvard University (US)
- ORCID
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2009-09-23
- Volume
- 111
- Issue
- 2
- Pages
- 417-427
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC2831412
- OpenAlex
- W2167574429
- Cited by
- 135
- References
- 33
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 3 · 2023: 4 · 2022: 6 · 2021: 8 · 2020: 10 · 2019: 3 · 2018: 10 · 2017: 7 · 2016: 10 · 2015: 8 · 2014: 10 · 2013: 11 · 2012: 18
- FWCI
- 8.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- Funders
- National Institute on Aging (R01AG026249, 2P50 AG05134, R01AG008487, P50AG005134, K99AG033670, P30AG062421)
- National Institute of Biomedical Imaging and Bioengineering (EB-00768, R01EB000768, P41EB002503)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau protein, tau isoforms, four-repeat tau, mitochondrial transport, axonal transport, retrograde transport, anterograde transport, microtubule binding, frontotemporal dementia, neurodegeneration, mitochondrial localization
- MeSH terms
- Animals, Axonal Transport, Cerebral Cortex, Glioma, Humans, Mitochondria, Neurons, Repetitive Sequences, Nucleic Acid, Transfection, tau Proteins, Protein Transport, Tauopathies, Cell Line, Tumor, Microfluidic Analytical Techniques, Green Fluorescent Proteins, Mice
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