Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-49669
Nat Commun 2014 Sep 29;5:5072. doi: 10.1038/ncomms6072.
Show Gene links Show Anatomy links

XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation.

Mortuza GB , Cavazza T , Garcia-Mayoral MF , Hermida D , Peset I , Pedrero JG , Merino N , Blanco FJ , Lyngsø J , Bruix M , Pedersen JS , Vernos I , Montoya G .


???displayArticle.abstract???
chTOG is a conserved microtubule polymerase that catalyses the addition of tubulin dimers to promote microtubule growth. chTOG interacts with TACC3, a member of the transforming acidic coiled-coil (TACC) family. Here we analyse their association using the Xenopus homologues, XTACC3 (TACC3) and XMAP215 (chTOG), dissecting the mechanism by which their interaction promotes microtubule elongation during spindle assembly. Using SAXS, we show that the TACC domain (TD) is an elongated structure that mediates the interaction with the C terminus of XMAP215. Our data suggest that one TD and two XMAP215 molecules associate to form a four-helix coiled-coil complex. A hybrid methods approach was used to define the precise regions of the TACC heptad repeat and the XMAP215 C terminus required for assembly and functioning of the complex. We show that XTACC3 can induce the recruitment of larger amounts of XMAP215 by increasing its local concentration, thereby promoting efficient microtubule elongation during mitosis.

???displayArticle.pubmedLink??? 25262927
???displayArticle.pmcLink??? PMC4200520
???displayArticle.link??? Nat Commun


Species referenced: Xenopus
Genes referenced: ckap5 spr tacc3 tff3.7


???attribute.lit??? ???displayArticles.show???
References [+] :
Al-Bassam, Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding. 2007, Pubmed, Xenbase