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XTACC3–XMAP215 association reveals an asymmetric interaction promoting microtubule elongation

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  • Gulnahar B. Mortuza

    (Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group
    Macromolecular Crystallography Group, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

  • Tommaso Cavazza

    (Centre for Genomic Regulation (CRG)
    Universitat Pompeu Fabra (UPF))

  • 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
    Macromolecular Crystallography Group, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

  • Isabel Peset

    (Centre for Genomic Regulation (CRG)
    Universitat Pompeu Fabra (UPF))

  • 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
    IKERBASQUE, Basque Foundation for Science)

  • 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)
    Universitat Pompeu Fabra (UPF)
    Institució Catalana de Recerca i Estudis Avançats (ICREA))

  • Guillermo Montoya

    (Structural Biology and Biocomputing Programme, Spanish National Cancer Research Centre (CNIO), Macromolecular Crystallography Group
    Macromolecular Crystallography Group, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

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.

Suggested Citation

  • 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 Pederse, 2014. "XTACC3–XMAP215 association reveals an asymmetric interaction promoting microtubule elongation," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6072
    DOI: 10.1038/ncomms6072
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