XTACC3–XMAP215 association reveals an asymmetric interaction promoting microtubule elongation

Gulnahar B. Mortuza (), Tommaso Cavazza, Maria Flor Garcia-Mayoral, Dario Hermida, Isabel Peset, Juan G. Pedrero, Nekane Merino, Francisco J. Blanco, Jeppe Lyngsø, Marta Bruix, Jan Skov Pedersen, Isabelle Vernos () and Guillermo Montoya ()
Additional contact information
Gulnahar B. Mortuza: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group
Tommaso Cavazza: Centre for Genomic Regulation (CRG)
Maria Flor Garcia-Mayoral: Spanish National Research Council (CSIC), Institute of Physical Chemistry ‘Rocasolano’
Dario Hermida: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group
Isabel Peset: Centre for Genomic Regulation (CRG)
Juan G. Pedrero: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group
Nekane Merino: Structural Biology Unit, CIC bioGUNE
Francisco J. Blanco: Structural Biology Unit, CIC bioGUNE
Jeppe Lyngsø: Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry Aarhus University
Marta Bruix: Spanish National Research Council (CSIC), Institute of Physical Chemistry ‘Rocasolano’
Jan Skov Pedersen: Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry Aarhus University
Isabelle Vernos: Centre for Genomic Regulation (CRG)
Guillermo Montoya: Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6072

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