XTACC3-XMAP215 association reveals an asymmetric interaction promoting
microtubule elongation

Mortuza, Gulnahar; Cavazza, Tommaso, 1985-; García Mayoral, María Flor; Hermida, Dario; Peset, Isabel; Pedrero, Juan G.; Merino, Nekane; Blanco, Francisco; Lyngsø, Jeppe; Bruix, Marta; Pedersen, Jan Skov; Vernos, Isabelle, 1959-; Montoya, Guillermo

XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation

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dc.contributor.author Mortuza, Gulnahar
dc.contributor.author Cavazza, Tommaso, 1985-
dc.contributor.author García Mayoral, María Flor
dc.contributor.author Hermida, Dario
dc.contributor.author Peset, Isabel
dc.contributor.author Pedrero, Juan G.
dc.contributor.author Merino, Nekane
dc.contributor.author Blanco, Francisco
dc.contributor.author Lyngsø, Jeppe
dc.contributor.author Bruix, Marta
dc.contributor.author Pedersen, Jan Skov
dc.contributor.author Vernos, Isabelle, 1959-
dc.contributor.author Montoya, Guillermo
dc.date.accessioned 2020-12-01T08:02:46Z
dc.date.available 2020-12-01T08:02:46Z
dc.date.issued 2014
dc.description.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.
dc.format.mimetype application/pdf
dc.identifier.citation 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. XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation. Nat Commun. 2014; 5:5072. DOI: 10.1038/ncomms607
dc.identifier.doi http://dx.doi.org/10.1038/ncomms607
dc.identifier.issn 2041-1723
dc.identifier.uri http://hdl.handle.net/10230/45915
dc.language.iso eng
dc.publisher Nature Research
dc.relation.ispartof Nat Commun. 2014; 5:5072
dc.rights This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.rights.uri http://creativecommons.org/licenses/by/4.0/
dc.subject.keyword Microtubules
dc.subject.keyword Proteins
dc.subject.keyword Structural biology
dc.title XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation
dc.type info:eu-repo/semantics/article
dc.type.version info:eu-repo/semantics/publishedVersion

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