Benoît Gigant

TL;DR: Changes in the subunits of tubulin as it switches from its straight conformation to a curved one correlate with the loss of lateral contacts and provide a rationale for the rapid microtubule depolymerization characteristic of dynamic instability.

TL;DR: The X-ray structure of vinblastine bound to tubulin in a complex with the RB3 protein stathmin-like domain (RB3-SLD) explains vin Blastine-induced tubulin self-association into spiral aggregates at the expense of microtubule growth.

TL;DR: The structure of the complex of GDP-tubulin with the stathmin-like domain of the neural protein RB3 reveals a head-to-tail assembly of two tubulins with a 91-residue RB3 alpha helix in which each copy of an internal duplicated sequence interacts with a different tubulin.

TL;DR: The structures of tubulin complexed with a set of colchicine site ligands are determined and it is suggested that the interference with microtubule assembly gets frozen, and the β-subunit T7 loop participates in a reversible way in the resistance to straightening that opposes micro Tubulin assembly.

TL;DR: Crystallographic, NMR, and mutagenetic data reveal that the weaker interaction of the C-terminal region of beta-thymosin/WH2 domain with actin accounts for the switch in function from inhibition to promotion of actin assembly.