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The tubulin cofactor C family member TBCCD1 orchestrates cytoskeletal filament formation

Andre, J., Harrison, S., Towers, K., Qi, X., Vaughan, S., McKean, P. G. and Ginger, Michael L. (2013) The tubulin cofactor C family member TBCCD1 orchestrates cytoskeletal filament formation. Journal of Cell Science, 126 (23). pp. 5350-5356. ISSN 0021-9533

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Abstract

TBCCD1 is an enigmatic member of the tubulin-binding cofactor C (TBCC) family of proteins required for mother–daughter centriole linkage in the green alga Chlamydomonas reinhardtii and nucleus–centrosome–Golgi linkage in mammalian cells. Loss of these linkages has severe morphogenetic consequences, but the mechanism(s) through which TBCCD1 contributes to cell organisation is unknown. In the African sleeping sickness parasite Trypanosoma brucei a microtubule-dominant cytoskeleton dictates cell shape, influencing strongly the positioning and inheritance patterns of key intracellular organelles. Here, we show the trypanosome orthologue of TBCCD1 is found at multiple locations: centrioles, the centriole-associated Golgi ‘bi-lobe’, and the anterior end of the cell body. Loss of Trypanosoma brucei TBCCD1 results in disorganisation of the structurally complex bi-lobe architecture and loss of centriole linkage to the single unit-copy mitochondrial genome (or kinetoplast) of the parasite. We therefore identify TBCCD1 as an essential protein associated with at least two filament-based structures in the trypanosome cytoskeleton. The last common ancestor of trypanosomes, animals and green algae was arguably the last common ancestor of all eukaryotes. On the basis of our observations, and interpretation of published data, we argue for an unexpected co-option of the TBCC domain for an essential non-tubulin-related function at an early point during evolution of the eukaryotic cytoskeleton.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Schools: School of Applied Sciences
Related URLs:
Depositing User: Michael Ginger
Date Deposited: 09 May 2016 13:06
Last Modified: 04 Dec 2016 04:54
URI: http://eprints.hud.ac.uk/id/eprint/28244

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