2026-06-14T06:44:11Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/114032024-11-30T00:41:34Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597

00925njm 22002777a 4500 dc Mortuza, Gulnahar B author Cavazza, Tommaso author Garcia-Mayoral, Maria Flor author Hermida, Dario author Peset, Isabel author Pedrero, Juan G author Merino, Nekane author Blanco, Francisco J author Lyngsø, Jeppe author Bruix, Marta author Pedersen, Jan Skov author Vernos, Isabelle author Montoya, Guillermo author 2014-09-29 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. Nat Commun . 2014;5:5072. 10.1038/ncomms6072 2041-1723 Nature communications 25262927 http://hdl.handle.net/20.500.12105/11403 XTACC3-XMAP215 association reveals an asymmetric interaction promoting microtubule elongation.