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The extended tubulin superfamily

School of Biological Sciences, University of Manchester, 2.205 Stopford Building, Oxford Road, Manchester M13 9PT, UK
^* Author for correspondence (e-mail: k.gull{at}man.ac.uk )

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.

Key words: Tubulin, Cytoskeleton, Microtubule, Flagellum, FtsZ, Evolution

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