Home > Research > Publications & Outputs > Tubulin-binding cofactor C domain-containing pr...

Links

Text available via DOI:

View graph of relations

Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation

Research output: Contribution to journalJournal articlepeer-review

Published

Standard

Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation. / Andre, Jane; Harrison, Stephanie; Towers, Katie; Qi, Xin; Vaughan, Sue; McKean, Paul; Ginger, Michael.

In: Journal of Cell Science, Vol. 126, 12.2013, p. 5350-5356.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Andre, J, Harrison, S, Towers, K, Qi, X, Vaughan, S, McKean, P & Ginger, M 2013, 'Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation', Journal of Cell Science, vol. 126, pp. 5350-5356. https://doi.org/10.1242/jcs.136515

APA

Andre, J., Harrison, S., Towers, K., Qi, X., Vaughan, S., McKean, P., & Ginger, M. (2013). Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation. Journal of Cell Science, 126, 5350-5356. https://doi.org/10.1242/jcs.136515

Vancouver

Author

Andre, Jane ; Harrison, Stephanie ; Towers, Katie ; Qi, Xin ; Vaughan, Sue ; McKean, Paul ; Ginger, Michael. / Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation. In: Journal of Cell Science. 2013 ; Vol. 126. pp. 5350-5356.

Bibtex

@article{eec505c4d55b41ceb7331c16e38132de,
title = "Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation",
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 TbTBCCD1 results in disorganisation of the structurally complex 'bi-lobe' architecture and loss of centriole linkage to the parasite's single unit-copy mitochondrial genome (or kinetoplast). 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. Based on our observations, and interpretation of published data, we argue for unexpected co-option of the TBCC domain for an essential, non-tubulin related function, at an early point during evolution of the eukaryotic cytoskeleton.",
keywords = "cytoskeleton, Golgi, Kinetoplast, TBCC domain, Trypnanosome",
author = "Jane Andre and Stephanie Harrison and Katie Towers and Xin Qi and Sue Vaughan and Paul McKean and Michael Ginger",
year = "2013",
month = dec,
doi = "10.1242/jcs.136515",
language = "English",
volume = "126",
pages = "5350--5356",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",

}

RIS

TY - JOUR

T1 - Tubulin-binding cofactor C domain-containing protein TBCCD1 orchestrates cytoskeletal filament formation

AU - Andre, Jane

AU - Harrison, Stephanie

AU - Towers, Katie

AU - Qi, Xin

AU - Vaughan, Sue

AU - McKean, Paul

AU - Ginger, Michael

PY - 2013/12

Y1 - 2013/12

N2 - 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 TbTBCCD1 results in disorganisation of the structurally complex 'bi-lobe' architecture and loss of centriole linkage to the parasite's single unit-copy mitochondrial genome (or kinetoplast). 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. Based on our observations, and interpretation of published data, we argue for unexpected co-option of the TBCC domain for an essential, non-tubulin related function, at an early point during evolution of the eukaryotic cytoskeleton.

AB - 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 TbTBCCD1 results in disorganisation of the structurally complex 'bi-lobe' architecture and loss of centriole linkage to the parasite's single unit-copy mitochondrial genome (or kinetoplast). 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. Based on our observations, and interpretation of published data, we argue for unexpected co-option of the TBCC domain for an essential, non-tubulin related function, at an early point during evolution of the eukaryotic cytoskeleton.

KW - cytoskeleton

KW - Golgi

KW - Kinetoplast

KW - TBCC domain

KW - Trypnanosome

U2 - 10.1242/jcs.136515

DO - 10.1242/jcs.136515

M3 - Journal article

VL - 126

SP - 5350

EP - 5356

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

ER -