The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Open accessAbstract
The subcellular distribution of microtubules containing acetylated alpha-tubulin in mammalian cells in culture was analyzed with 6-11B-1, a monoclonal antibody specific for acetylated alpha-tubulin. Cultures of 3T3, HeLa, and PtK2 cells were grown on coverslips and observed by immunofluorescence microscopy after double-staining by 6-11B-1 and B-5-1-2, a monoclonal antibody specific for all alpha-tubulins. The antibody 6-11B-1 binds to primary cilia, centrioles, mitotic spindles, midbodies, and to subsets of cytoplasmic microtubules in 3T3 and HeLa cells, but not in PtK2 cells. These observations confirm that the acetylation of alpha-tubulin is a modification occurring in different microtubule structures and in a variety of eukaryotic cells. Some features of the acetylation of cytoplasmic microtubules of mammalian cells are also described here. First, acetylated alpha-tubulin is present in microtubules that, under depolymerizing conditions, are more stable than the majority of cytoplasmic microtubules. In addition to the specific microtubule frameworks already mentioned, cytoplasmic microtubules resistant to nocodazole or colchicine, but not cold-resistant microtubules, contain more acetylated alpha-tubulin than the rest of cellular microtubules. Second, the alpha-tubulin in all cytoplasmic microtubules of 3T3 and HeLa cells becomes acetylated in the presence of taxol, a drug that stabilizes microtubules. Third, acetylation and deacetylation of cytoplasmic microtubules are reversible in cells released from exposure to 0 degrees C or antimitotic drugs. Fourth, the epitope recognized by the antibody 6-11B-1 is not absolutely necessary for cell growth and division. This epitope is absent in PtK2 cells. The acetylation of alpha-tubulin could regulate the presence of microtubules in specific intracellular spaces by selective stabilization.
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“A characteristic feature of stable MTs is their curved appearance (Piperno et al., 1987; Friedman et al., 2010; Katrukha et al., 2017).”
From A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle (2023) · cites this paper as Piperno et al., 1987
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“acetylated tubulin (AcTub) (Fig. 5a), a marker for stable microtubules [29]”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [29]
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“Acetylation in interphase cells typically occurs on stable microtubules 37,38 , and stable microtubules were recently found to have a distinct, expanded lattice conformation 39 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [37]
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Cites
Taxol stabilizes microtubules in mouse fibroblast cells.
Schiff, P. B., & Horwitz, S. B. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1561 · Cited by 1,971
Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758
Self-citationTaxol binds to polymerized tubulin in vitro
Parness, J., & Horwitz, S. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.2.479 · Cited by 624
L’Hernault, S. W., & Rosenbaum, J. L. (1985) · Biochemistry · doi:10.1021/bi00323a034 · Cited by 497
Microtubule dynamics in interphase cells
Schulze, E., & Kirschner, M. (1986) · The Journal of cell biology · doi:10.1083/jcb.102.3.1020 · Cited by 335
L’Hernault, S. W., & Rosenbaum, J. L. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.1.258 · Cited by 255
A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters.
Jahn, R., SCHIEBLER, W., & Greengard, P. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.6.1684 · Cited by 244
Ledizet, M., & Piperno, G. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.1.13 · Cited by 204
Self-citationL’Hernault, S. W., & Rosenbaum, J. L. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.2.457 · Cited by 88
Linck, R. W., Amos, L., & Amos, W. B. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.126 · Cited by 85
Cited by
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HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542
The Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,497
Plasticity of cell migration: a multiscale tuning model
Friedl, P., & Wolf, K. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200909003 · Cited by 1,356
High-Resolution Model of the Microtubule
Nogales, E., Whittaker, M., Milligan, R. A., & Downing, K. H. (1999) · Cell · doi:10.1016/s0092-8674(00)80961-7 · Cited by 1,200
Metadata
- Authors
- Piperno, G., LeDizet, M., & Chang, X. J.
- Affiliations
- Rockefeller University (US)
- ORCID
- LeDizet, M
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1987-02-01
- Volume
- 104
- Issue
- 2
- Pages
- 289-302
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2114420
- OpenAlex
- W2155768517
- Cited by
- 873
- References
- 13
- Citations by year
- 2026: 15 · 2025: 18 · 2024: 23 · 2023: 27 · 2022: 19 · 2021: 30 · 2020: 24 · 2019: 29 · 2018: 32 · 2017: 28 · 2016: 28 · 2015: 34 · 2014: 33 · 2013: 34 · 2012: 36
- FWCI
- 15.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM28702)
- National Center for Research Resources (S07 RR077065)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- acetylated alpha-tubulin, alpha-tubulin acetylation, microtubules, cytoplasmic microtubules, primary cilia, centrioles, mitotic spindle, midbody, microtubule stabilization, paclitaxel, nocodazole, colchicine, deacetylation, 3T3 fibroblasts, HeLa cells, PtK2 cells
- MeSH terms
- Acetylation, Alkaloids, Animals, Cell Line, Cells, Cultured, Cold Temperature, Fluorescent Antibody Technique, HeLa Cells, Humans, Kinetics, Microtubules, Tubulin, Paclitaxel, Mice
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