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XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation

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  • Gulnahar B. Mortuza, Spanish Natl Canc Res Ctr CNIO, Spanish National Cancer Research Centre, Macromol Crystallog Grp, Struct Biol & Biocomp Programme, Ukendt
  • Tommaso Cavazza, Ctr Genom Regulat CRG, Centre for Genomic Regulation - CRG, Pompeu Fabra University, Ukendt
  • Maria Flor Garcia-Mayoral, CSIC, Consejo Superior de Investigaciones Cientificas (CSIC), Spanish Natl Res Council, Inst Phys Chem Rocasolano, Dept Biol Phys Chem, Ukendt
  • Dario Hermida, Spanish Natl Canc Res Ctr CNIO, Spanish National Cancer Research Centre, Macromol Crystallog Grp, Struct Biol & Biocomp Programme, Ukendt
  • Isabel Peset, Ctr Genom Regulat CRG, Centre for Genomic Regulation - CRG, Pompeu Fabra University, Ukendt
  • Juan G. Pedrero, Spanish Natl Canc Res Ctr CNIO, Spanish National Cancer Research Centre, Macromol Crystallog Grp, Struct Biol & Biocomp Programme, Ukendt
  • Nekane Merino, CIC BioGUNE, Struct Biol Unit, Spanien
  • Francisco J. Blanco, CIC BioGUNE, Struct Biol Unit, Spanien
  • Jeppe Lyngso, Danmark
  • Marta Bruix, CSIC, Consejo Superior de Investigaciones Cientificas (CSIC), Spanish Natl Res Council, Inst Phys Chem Rocasolano, Dept Biol Phys Chem, Ukendt
  • Jan Skov Pedersen
  • Isabelle Vernos, Ctr Genom Regulat CRG, Centre for Genomic Regulation - CRG, Pompeu Fabra University, Ukendt
  • Guillermo Montoya, Spanish Natl Canc Res Ctr CNIO, Spanish National Cancer Research Centre, Macromol Crystallog Grp, Struct Biol & Biocomp Programme, Ukendt
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.
OriginalsprogEngelsk
Artikelnummer5072
TidsskriftNature Communications
Vol/bind5
Antal sider12
ISSN2041-1723
DOI
StatusUdgivet - 2014

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