XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation
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XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. / Mortuza, Gulnahar B; Cavazza, Tommaso; Garcia-Mayoral, Maria Flor; Hermida, Dario; Peset, Isabel; Pedrero, Juan G; Merino, Nekane; Blanco, Francisco J; Lyngsø, Jeppe; Bruix, Marta; Pedersen, Jan Skov; Vernos, Isabelle; Montoya, Guillermo.
In: Nature Communications, Vol. 5, 5072, 29.09.2014, p. 1-12.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation
AU - Mortuza, Gulnahar B
AU - Cavazza, Tommaso
AU - Garcia-Mayoral, Maria Flor
AU - Hermida, Dario
AU - Peset, Isabel
AU - Pedrero, Juan G
AU - Merino, Nekane
AU - Blanco, Francisco J
AU - Lyngsø, Jeppe
AU - Bruix, Marta
AU - Pedersen, Jan Skov
AU - Vernos, Isabelle
AU - Montoya, Guillermo
PY - 2014/9/29
Y1 - 2014/9/29
N2 - 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.
AB - 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.
U2 - 10.1038/ncomms6072
DO - 10.1038/ncomms6072
M3 - Journal article
C2 - 25262927
VL - 5
SP - 1
EP - 12
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 5072
ER -
ID: 138737834