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The extended tubulin superfamily.

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The extended tubulin superfamily. / McKean, Paul G.; Vaughan, Sue; Gull, Keith.

In: Journal of Cell Science, Vol. 114, No. 15, 08.2001, p. 2723-2733.

Research output: Contribution to journalJournal articlepeer-review

Harvard

McKean, PG, Vaughan, S & Gull, K 2001, 'The extended tubulin superfamily.', Journal of Cell Science, vol. 114, no. 15, pp. 2723-2733. <http://jcs.biologists.org/cgi/content/abstract/114/15/2723>

APA

McKean, P. G., Vaughan, S., & Gull, K. (2001). The extended tubulin superfamily. Journal of Cell Science, 114(15), 2723-2733. http://jcs.biologists.org/cgi/content/abstract/114/15/2723

Vancouver

McKean PG, Vaughan S, Gull K. The extended tubulin superfamily. Journal of Cell Science. 2001 Aug;114(15):2723-2733.

Author

McKean, Paul G. ; Vaughan, Sue ; Gull, Keith. / The extended tubulin superfamily. In: Journal of Cell Science. 2001 ; Vol. 114, No. 15. pp. 2723-2733.

Bibtex

@article{f9b701226a0b491388c93a7ed9a13320,
title = "The extended tubulin superfamily.",
abstract = "Although most eukaryotic cells can express multiple isotypes of {\ss}-tubulin, the significance of this diversity has not always been apparent. Recent data indicate that particular {\ss}-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, , , , and , have been identified. Although the role of -tubulin in the nucleation of microtubule assembly is now well established, far less is known about the functions of -, -, - and -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 -, -, - and -tubulin all have functions associated with the centriole or basal body of eukaryotic cells and organisms.",
keywords = "Tubulin, Cytoskeleton, Microtubule, Flagellum, FtsZ, Evolution",
author = "McKean, {Paul G.} and Sue Vaughan and Keith Gull",
year = "2001",
month = aug,
language = "English",
volume = "114",
pages = "2723--2733",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
number = "15",

}

RIS

TY - JOUR

T1 - The extended tubulin superfamily.

AU - McKean, Paul G.

AU - Vaughan, Sue

AU - Gull, Keith

PY - 2001/8

Y1 - 2001/8

N2 - Although most eukaryotic cells can express multiple isotypes of ß-tubulin, the significance of this diversity has not always been apparent. Recent data indicate that particular ß-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, , , , and , have been identified. Although the role of -tubulin in the nucleation of microtubule assembly is now well established, far less is known about the functions of -, -, - and -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 -, -, - and -tubulin all have functions associated with the centriole or basal body of eukaryotic cells and organisms.

AB - Although most eukaryotic cells can express multiple isotypes of ß-tubulin, the significance of this diversity has not always been apparent. Recent data indicate that particular ß-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, , , , and , have been identified. Although the role of -tubulin in the nucleation of microtubule assembly is now well established, far less is known about the functions of -, -, - and -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 -, -, - and -tubulin all have functions associated with the centriole or basal body of eukaryotic cells and organisms.

KW - Tubulin

KW - Cytoskeleton

KW - Microtubule

KW - Flagellum

KW - FtsZ

KW - Evolution

M3 - Journal article

VL - 114

SP - 2723

EP - 2733

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 15

ER -