Tau Is Enriched on Dynamic Microtubules in the Distal Region of Growing Axons
Open accessAbstract
It is widely held that tau determines the stability of microtubules in growing axons, although direct evidence supporting this hypothesis is lacking. Previous studies have shown that the microtubule polymer in the distal axon and growth cone is the most dynamic of growing axons; it turns over more rapidly and is more sensitive to microtubule depolymerizing drugs than the polymer situated proximally. We reasoned that if the stability of axonal microtubules is directly related to their content of tau, then the polymer in the distal axon should have less tau than the polymer in the proximal axon. We tested this proposition by measuring the relative tau content of microtubules along growing axons of cultured sympathetic neurons immunostained for tau and tubulin. Our results show that the tau content of microtubules varies along the axon, but in the opposite way predicted. Specifically, the relative tau content of microtubules increases progressively along the axon to reach a peak near the growth cone that is severalfold greater than that observed proximally. Thus, tau is most enriched on the most dynamic polymer of the axon. We also show that the gradient in tau content of microtubules does not generate corresponding gradients in the extent of tubulin assembly or in the sensitivity of axonal microtubules to nocodazole. On the basis of these findings, we propose that tau in growing axons has functions other than promoting microtubule assembly and stability and that key sites for these functions are the distal axon and growth cone.
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Tau has been found on dynamic microtubules in the actin rich growth cone areas of developing neurons.
“Tau has also been found on dynamic microtubules in the actin rich growth cone areas of developing neurons71.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [71]
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- Tucker RP (1990) The role of microtubule-associated proteins in brain morphogcnesis: a review. Brain Res Rev 15:109-120.
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- Authors
- Black, M. M., Slaughter, T., Moshiach, S., Obrocka, M., & Fischer, I.
- Affiliations
- Temple University (US)
- ORCID
- Fischer, Itzhak
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1996-06-01
- Volume
- 16
- Issue
- 11
- Pages
- 3601-3619
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6578833
- OpenAlex
- W2111537613
- Cited by
- 270
- References
- 1
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 5 · 2023: 20 · 2022: 12 · 2021: 11 · 2020: 20 · 2019: 8 · 2018: 10 · 2017: 13 · 2016: 13 · 2015: 6 · 2014: 7 · 2013: 4 · 2012: 6
- FWCI
- 3.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (NS 24707, R01NS017681, R01NS024275, P50NS024707, NS 17681, NS24275)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau protein, axonal microtubules, microtubule dynamics, axon growth, growth cones, sympathetic neurons, microtubule stability, tubulin assembly
- MeSH terms
- Adrenergic Fibers, Animals, Antibody Specificity, Axons, Base Sequence, Cells, Cultured, Detergents, Fixatives, Fluorescent Antibody Technique, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Neurons, Polymers, Recombinant Proteins, Tubulin, Polymerase Chain Reaction, Neurites, tau Proteins, Superior Cervical Ganglion, Rats
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