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Nat Commun. 2014 Sep 29;5:5072. doi: 10.1038/ncomms6072.

Autores

Gulnahar B. Mortuza ,TommasoCavazza, Maria Flor Garcia-Mayoral, Dario Hermida, Isabel Peset, Juan G. Pedrero, Nekane Merino, Francisco J. Blanco, JeppeLyngsø, Marta Bruix, Jan Skov Pedersen, Isabelle Vernos& Guillermo Montoya

Resumen

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. DOI: 10.10

Descripción

Investigadores del equipo de Guillermo Montoya en el Centro Nacional de Investigaciones Oncológicas (CNIO) han descifrado, en colaboración con el Grupo de Isabelle Vernos en el Centro de Regulación Genómica (CRG), la interacción molecular entre TACC3 y chTOG, proteínas clave para la formación del andamiaje interno celular que posibilita y sustenta la división de las células. Las observaciones, publicadas en Nature Communications, podrían ayudar a optimizar las terapias oncológicas actuales dirigidas específicamente contra este andamiaje, bautizado por la comunidad científica con el nombre de microtubules.

grupo

REFERENCIA DEL GRUPO INVESTIGADOR

Este trabajo se llevó a cabo en el CNIO, España. Sin embargo, recientemente los miembros del laboratorio de Guillermo Montoya que trabajan en este proyecto se trasladaron con él a Novo Nordisk Foundation Centre for Protein Research (NNF-CPR), Copenhague, y seguirán investigando la estructura y función de las proteínas y sus complejos en la mitosis.

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