Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/31740
Title: TACC3-ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation.
Authors: Gutiérrez-Caballero, C.
Burgess, Selena G.
Bayliss, Richard
Royle, Stephen J.
First Published: 16-Jan-2015
Citation: Biol Open, February 2015, 4, 170-179.
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 mitotic 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. Recent work indicates that TACC3 can track the plus-ends of microtubules and modulate microtubule dynamics in non-dividing cells via its interaction with ch-TOG. 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 describe the molecular interaction between TACC3 and ch-TOG that permits TACC3 recruitment to the plus-ends of microtubules. This TACC3-ch-TOG pool is independent of EB1, EB3, Aurora-A phosphorylation and binding to clathrin. We also describe the distinct combinatorial 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.
DOI Link: 10.1242/bio.201410843
ISSN: 2046-6390
eISSN: 2046-6390
Links: http://bio.biologists.org/content/4/2/170
http://hdl.handle.net/2381/31740
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
Appears in Collections:Published Articles, Dept. of Biochemistry

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