Axonal tubulin and axonal microtubules: biochemical evidence for cold stability
Open accessAbstract
Nerve extracts containing tubulin labeled by axonal transport were analyzed by electrophoresis and differential extraction. We found that a substantial fraction of the tubulin in the axons of the retinal ganglion cell of guinea pigs is not solubilized by conventional methods for preparation of microtubules from whole brain. In two-dimensional polyacrylamide gel electrophoresis this cold-insoluble tubulin was biochemically distinct from tubulin obtained from whole brain microtubules prepared by cold cycling. Cleveland peptide maps also indicated some differences between the cold-extractable and cold-insoluble tubulins. The demonstration of cold-insoluble tubulin that is specifically axonal in origin permits consideration of the physiological role of cold-insoluble tubulin in a specific cellular structure. It appears likely that much of this material is in the form of cold-stable microtubules. We propose that the physiological role of cold-insoluble tubulin in the axon may be associated with the regulation of the axonal microtubule complexes in neurons.
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Axonal microtubules are considered to be highly stable.
“While axonal microtubules are considered to be highly stable (Black et al., 1984; Brady et al., 1984; Sahenk and Brady, 1987; Lim et al., 1989; Okabe and Hirokawa, 1990; Baas et al., 1991; Ahmad et al., 1993; Li and Black, 1996; Song et al., 2013)”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Brady et al., 1984
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Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167 · see citing works
Guillaud, L., Bosc, C., Fourest-Lieuvin, A., Denarier, E., Pirollet, F., Lafanechère, L., & Job, D. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.167 · Cited by 132 · see citing works
Beaudet, D., Berger, C. L., & Hendricks, A. G. (2026) · eLife · doi:10.7554/elife.110011
- Authors
- Brady, S. T., Tytell, M., & Lasek, R. J.
- Affiliations
- Case Western Reserve University (US)
- ORCID
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1984-11-01
- Volume
- 99
- Issue
- 5
- Pages
- 1716-1724
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2113352
- OpenAlex
- W2138948965
- Cited by
- 170
- References
- 0
- Citations by year
- 2026: 4 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 7 · 2020: 2 · 2019: 2 · 2018: 1 · 2017: 5 · 2016: 3 · 2015: 3 · 2014: 3 · 2013: 4 · 2012: 1
- FWCI
- 6.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- axonal microtubules, cold stability, retinal ganglion cells, axonal transport, axon cytoskeleton, guinea pig
- MeSH terms
- Animals, Axons, Calcium, Cold Temperature, Electrophoresis, Polyacrylamide Gel, Guinea Pigs, Isoelectric Focusing, Male, Microtubules, Molecular Weight, Rats, Inbred Strains, Retina, Retinal Ganglion Cells, Solubility, Tubulin, Rats
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