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TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation
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Gutierrez-Caballero, Cristina, Burgess, Selena G., Bayliss, Richard and Royle, Stephen J. (2015) TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation. Biology Open, 4 . pp. 170-179. doi:10.1242/bio.201410843 ISSN 2046-6390.
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Official URL: http://dx.doi.org/10.1242/bio.201410843
Abstract
The interaction between TACC3 (transforming acidic coiled coil protein 3) and the microtubule polymerase ch-TOG (colonic, hepatic tumor overexpressed gene) is evolutionarily conserved. Loading of TACC3–ch-TOG onto spindle microtubules requires the phosphorylation of TACC3 by Aurora-A kinase and the subsequent interaction of TACC3 with clathrin to form a microtubule binding surface. Whether there is a pool of TACC3–ch-TOG that is independent of clathrin in human cells, and what is the function of this pool, are open questions. Here, we report that TACC3 is recruited to the plus-ends of microtubules by its association with ch-TOG and that this pool is independent of phosphorylation and binding to clathrin. The plus-end binding of TACC3–ch-TOG persists in interphase and we propose that one cellular function of TACC3–ch-TOG is to modulate cell migration. We also describe the distinct subcellular pools of TACC3, ch-TOG and clathrin. TACC3 is often described as a centrosomal protein, but we show that there is no significant population of TACC3 at centrosomes. The delineation of distinct protein pools reveals a simplified view of how these proteins are organized and controlled by post-translational modification.
Item Type: | Journal Article | ||||||||||
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Subjects: | Q Science > QR Microbiology | ||||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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Library of Congress Subject Headings (LCSH): | Microtubules, Rho-associated protein kinases | ||||||||||
Journal or Publication Title: | Biology Open | ||||||||||
Publisher: | The Company of Biologists Ltd. | ||||||||||
ISSN: | 2046-6390 | ||||||||||
Official Date: | 2015 | ||||||||||
Dates: |
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Volume: | 4 | ||||||||||
Number of Pages: | 10 | ||||||||||
Page Range: | pp. 170-179 | ||||||||||
DOI: | 10.1242/bio.201410843 | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||||||
Date of first compliant deposit: | 28 July 2016 | ||||||||||
Date of first compliant Open Access: | 28 July 2016 | ||||||||||
Funder: | Cancer Research UK (CRUK), Warwick Medical School | ||||||||||
Grant number: | C25425/ A15182 (CRUK), C24461/A12772 (CRUK) |
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