XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Mortuza, GB, Cavazza, T, Garcia-Mayoral, MF, Hermida, D, Peset, I, Pedrero, JG, Merino, N, Blanco, FJ, Lyngsø, J, Bruix, M, Pedersen, JS, Vernos, I & Montoya, G 2014, 'XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation', Nature Communications, vol. 5, 5072, pp. 1-12. https://doi.org/10.1038/ncomms6072

APA

Mortuza, G. B., Cavazza, T., Garcia-Mayoral, M. F., Hermida, D., Peset, I., Pedrero, J. G., Merino, N., Blanco, F. J., Lyngsø, J., Bruix, M., Pedersen, J. S., Vernos, I., & Montoya, G. (2014). XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. Nature Communications, 5, 1-12. [5072]. https://doi.org/10.1038/ncomms6072

Vancouver

Mortuza GB, Cavazza T, Garcia-Mayoral MF, Hermida D, Peset I, Pedrero JG et al. XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. Nature Communications. 2014 Sep 29;5:1-12. 5072. https://doi.org/10.1038/ncomms6072

Author

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. / XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. In: Nature Communications. 2014 ; Vol. 5. pp. 1-12.

Bibtex

@article{91cb7cb0900e4f8b82d0c099f6403ef2,
title = "XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation",
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.",
author = "Mortuza, {Gulnahar B} and Tommaso Cavazza and Garcia-Mayoral, {Maria Flor} and Dario Hermida and Isabel Peset and Pedrero, {Juan G} and Nekane Merino and Blanco, {Francisco J} and Jeppe Lyngs{\o} and Marta Bruix and Pedersen, {Jan Skov} and Isabelle Vernos and Guillermo Montoya",
year = "2014",
month = sep,
day = "29",
doi = "10.1038/ncomms6072",
language = "English",
volume = "5",
pages = "1--12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

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