Cited by 129Microtubule and mitosis dynamicsAlzheimer's disease research and treatmentsCancer Treatment and Pharmacology

Tau interaction with microtubules in vivo

Open access
Samsonov, Andrey, Yu, Jiang-Zhou, Rasenick, Mark, Popov, Sergey V.·2004·Journal of Cell Science

Abstract

Tau is a major microtubule-associated protein which induces bundling and stabilization of axonal microtubules (MTs). To investigate the interaction of tau with MTs in living cells, we expressed GFP-tau fusion protein in cultured Xenopus embryo neurons and performed time-lapse imaging of tau-labeled MTs. Tau uniformly labeled individual MTs regardless of their assembly/disassembly status and location along the axon. Photobleaching experiments indicated that interaction of tau with MTs is very dynamic, with a half-time of fluorescence recovery of the order of 3 seconds. Treatment of cells with taxol, a drug that suppresses MT dynamics, rapidly induced detachment of tau from MTs. Although binding of tau to straight MTs was uniform, there was a heightened concentration of tau at the sites of high MT curvature. Our results suggest that dynamic interaction of tau with MTs may modify local mechanical properties of individual MTs and play a crucial role in the remodeling of the MT cytoskeleton during neuronal plasticity.

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  • In the remaining 6% of cells, exhibiting weak eGFP-tau expression, tau only localized to the microtubule bends.

    “In the remaining 6% of cells, exhibiting weak eGFP-tau expression, tau only localized to the microtubule bends, as described previously33,34.”

    From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [33]

    In “Binding of tau to individual MTs depends on their curvature” (page unavailable), the paper reports more GFP-tau at highly curved regions. It also reports GFP-tau labeling on relatively straight microtubules, so localization was not limited to bends. The passages do not support the figure of 6% of cells with weak expression. (LLM, conf=0.86)

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  • After adding 0.01 μM taxol to U-2 OS cells, tau dissociated from microtubules in all cells, as quantified by a decrease in the coefficient of variation of the tau signal.

    “We added 0.01 μM taxol to the medium and imaged the cells for 10 minutes while monitoring the tau density on microtubules initially fully covered by eGFP-tau. In line with our in vitro observations, and previous in vivo evidence33,35, we observed that in all cells tau dissociated from the microtubules (Fig. 4a, Supplementary Movie 9) as quantified by the decrease in the coefficient of variation of”

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Research works printed but not linked: 6

  1. D'Souza, I., Poorkaj, P., Hong, M., Nochlin, D., Lee, V. M., Bird, T. D. and Schellenberg, G. D. (1999). Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements. Proc. Natl. Acad. Sci. USA 96, 5598-5603.
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  3. Makrides, V., Massie, M. R., Feinstein, S. C. and Lew, J. (2004). Evidence for two distinct binding sites for tau on microtubules. Proc. Natl. Acad. Sci. USA 101, 6746-6751.
  4. Murphy, D. B. and Borisy, G. G. (1975). Association of high-molecular- weight proteins with microtubules and their role in microtubule assembly in vitro. Proc. Natl. Acad. Sci. USA 72, 2696-2700.
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Authors
Samsonov, A., Yu, J.-Z., Rasenick, M., & Popov, S. V.
Affiliations
University of Illinois Chicago (US)
Corresponding author
Popov, Sergey V.
Venue
Journal of Cell Science
Published
2004-12-01
Volume
117
Issue
25
Pages
6129-6141
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
OpenAlex
W2066025113
Cited by
129
References
3
Citations by year
2025: 3 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 4 · 2020: 7 · 2019: 6 · 2018: 8 · 2017: 7 · 2016: 11 · 2015: 6 · 2014: 9 · 2013: 9 · 2012: 13
FWCI
1.89
Type
journal article
Language
en
Open access
Locations
  • Journal of Cell Science (publishedVersion)
  • PubMed (publishedVersion)
  • HighWire Press Open Archive (submittedVersion)
Funders
  • National Institutes of Health (NS3350, NS39417)
  • National Institute of Neurological Disorders and Stroke (NS3350, NS39417, R01NS039417)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords
tau protein, microtubules, microtubule stabilization, microtubule bundling, axonal cytoskeleton, microtubule curvature, paclitaxel, microtubule dynamics, neuroplasticity
MeSH terms
Animals, Axons, Cytoskeleton, Detergents, DNA, Embryo, Nonmammalian, Fibroblasts, Image Processing, Computer-Assisted, Light, Microscopy, Fluorescence, Microtubules, Neurons, Protein Binding, Time Factors, Xenopus, tau Proteins, Paclitaxel, Green Fluorescent Proteins

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