Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding.
Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly and mitotic spindle binding.
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DOI:
10.1083/jcb.201211127
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发表时间:
2013-08-05
期刊:
影响因子:
--
通讯作者:
Royle SJ
中科院分区:
文献类型:
--
作者:
Hood FE;Williams SJ;Burgess SG;Richards MW;Roth D;Straube A;Pfuhl M;Bayliss R;Royle SJ
Aurora A phosphorylation-induced interaction of TACC3 and clathrin coordinates adjacent domains in each protein to create a microtubule-binding interface, whereas a distinct site in TACC3 recruits ch-TOG to mitotic spindles. Acomplex 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.
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影响因子:
10.5
作者:
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通讯作者:
Raff, JW
影响因子:
7.8
作者:
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DOI:
10.1083/jcb.201205116
发表时间:
2012-08-20
期刊:
The Journal of cell biology
影响因子:
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作者:
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通讯作者:
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DOI:
10.1007/978-1-61779-252-6_2
发表时间:
2011-01-01
期刊:
MICROTUBE DYNAMICS: METHODS AND PROTOCOLS
影响因子:
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作者:
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通讯作者:
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通讯作者:
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