Tubulin islands containing slowly hydrolyzable GTP analogs regulate the mechanism and kinetics of microtubule depolymerization.

ABSTRACT: Dynamic instability of microtubules is characterized by stochastically alternating phases of growth and shrinkage and is hypothesized to be controlled by the conformation and nucleotide state of tubulin dimers within the microtubule lattice. Specifically, conformation changes (compression) in the tubulin dimer following the hydrolysis of GTP have been suggested to generate stress and drive depolymerization. In the present study, molecular dynamics simulations were used in tandem with in vitro experiments to investigate changes in depolymerization based on the presence of islands of uncompressed (GMPCPP) dimers in the microtubule lattice. Both methods revealed an exponential decay in the kinetic rate of depolymerization corresponding to the relative level of uncompressed (GMPCPP) dimers, be

SUBMITTER: Bollinger JA 

PROVIDER: S-EPMC7423891 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature