title: The engine of microtubule dynamics comes into focus.
abstract: In this issue, Alushin et al. report high-resolution structures of three states of the microtubule lattice: GTP-bound, which is stable to depolymerization; unstable GDP-bound; and stable Taxol and GDP-bound. By comparing these structures at near-atomic resolution, they are able to propose a detailed model for how GTP hydrolysis destabilizes the microtubule and thus powers dynamic instability and chromosome movement. Destabilization of cytoskeleton filaments by nucleotide hydrolysis is an important general principle in cell dynamics, and this work represents a major step forward on a problem with a long history.
authors.affiliation: Deptartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: timothy_mitchison@hms.harvard.edu.
authors.forename: T J
authors.initials: TJ
authors.lastname: Mitchison
mesh_terms: D000818:Animals; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006801:Humans; D008870:Microtubules / Q000737:chemistry*; D014404:Tubulin / Q000737:chemistry*
chemical_list: D014404:Tubulin; D006160:Guanosine Triphosphate