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Title: Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding
Authors: Hood, F. E.
Williams, S. J.
Burgess, S. G.
Richards, M. W.
Roth, D.
Straube, A.
Pfuhl, M.
Bayliss, Richard William Anthony
Royle, S. J.
First Published: 5-Aug-2013
Publisher: Rockefeller University Press
Citation: Journal of Cell Biology, 2013, 202 (3), pp. 463-478
Abstract: A complex of transforming acidic coiled-coil protein 3 (TACC3), colonic and hepatic tumor overexpressed gene (ch-TOG), and clathrin has been implicated in mitotic spindle assembly and in the stabilization of kinetochore fibers by cross-linking microtubules. It is unclear how this complex binds microtubules and how the proteins in the complex interact with one another. TACC3 and clathrin have each been proposed to be the spindle recruitment factor. We have mapped the interactions within the complex and show that TACC3 and clathrin were interdependent for spindle recruitment, having to interact in order for either to be recruited to the spindle. The N-terminal domain of clathrin and the TACC domain of TACC3 in tandem made a microtubule interaction surface, coordinated by TACC3-clathrin binding. A dileucine motif and Aurora A-phosphorylated serine 558 on TACC3 bound to the "ankle" of clathrin. The other interaction within the complex involved a stutter in the TACC3 coiled-coil and a proposed novel sixth TOG domain in ch-TOG, which was required for microtubule localization of ch-TOG but not TACC3-clathrin.
DOI Link: 10.1083/jcb.201211127
ISSN: 0021-9525
eISSN: 1540-8140
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2013 Hood et al. This article is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at
Appears in Collections:Published Articles, College of Medicine, Biological Sciences and Psychology

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