RT Journal Article
SR Electronic
T1 TACC3–ch-TOG track the growing tips of microtubules independently of clathrin and Aurora-A phosphorylation
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 008359
DO 10.1101/008359
A1 Cristina Gutiérrez-Caballero
A1 Selena G. Burgess
A1 Richard Bayliss
A1 Stephen J. Royle
YR 2014
UL http://biorxiv.org/content/early/2014/08/21/008359.abstract
AB 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.