McKean, Paul G. and Vaughan, Sue and Gull, Keith (2001) The extended tubulin superfamily. Journal of Cell Science, 114 (15). pp. 2723-2733. ISSN 0021-9533Full text not available from this repository.
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.
|Journal or Publication Title:||Journal of Cell Science|
|Uncontrolled Keywords:||Tubulin ; Cytoskeleton ; Microtubule ; Flagellum ; FtsZ ; Evolution|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited By:||Dr Paul G McKean|
|Deposited On:||02 Jun 2008 13:47|
|Last Modified:||04 Nov 2015 03:03|
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