The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
The extended tubulin superfamily
Abstract
Although most eukaryotic cells can express multiple isotypes of αβ-tubulin, the significance of this diversity has not always been apparent. Recent data indicate that particular αβ-tubulin isotypes, both genome encoded and those derived by post-translational modification, can directly influence microtubule structure and function — thus validating ideas originally proposed in the multitubulin hypothesis over 25 years ago. It has also become increasingly evident over the past year that some (but intriguingly not all) eukaryotes encode several other tubulin proteins, and to date five further members of the tubulin superfamily, γ, δ, ϵ, 𝛇 and η, have been identified. Although the role of γ-tubulin in the nucleation of microtubule assembly is now well established, far less is known about the functions of δ-, ϵ-, 𝛇- and η-tubulin. Recent work has expanded our knowledge of the functions and localisation of these newer members of the tubulin superfamily, and the emerging data suggesting a restricted evolutionary distribution of these `new' tubulin proteins, conforms to established knowledge of microtubule cell biology. On the basis of current evidence, we predict that δ-, ϵ-, 𝛇- and η-tubulin all have functions associated with the centriole or basal body of eukaryotic cells and organisms.
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Cites
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Cited by
Post-translational modifications regulate microtubule function
Westermann, S., & Weber, K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1260 · Cited by 717
Microtubules and Microtubule-Associated Proteins
Goodson, H. V., & Jonasson, E. M. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022608 · Cited by 579
Drugs that target dynamic microtubules: A new molecular perspective
Stanton, R. A., Gernert, K. M., Nettles, J. H., & Aneja, R. (2011) · Medicinal Research Reviews · doi:10.1002/med.20242 · Cited by 526
Assembly of centrosomal proteins and microtubule organization depends on PCM-1
Dammermann, A., & Merdes, A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204023 · Cited by 489
Microtubules, microtubule-interfering agents and apoptosis
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Metadata
- Authors
- McKean, P. G., Vaughan, S., & Gull, K.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2001-08-01
- Volume
- 114
- Issue
- 15
- Pages
- 2723-2733
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1913492258
- Cited by
- 265
- References
- 58
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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