Structural mass spectrometry of the alpha beta-tubulin dimer supports a revised model of microtubule assembly.

ABSTRACT: The molecular basis of microtubule lattice instability derives from the hydrolysis of GTP to GDP in the lattice-bound state of alphabeta-tubulin. While this has been appreciated for many years, there is ongoing debate over the molecular basis of this instability and the possible role of altered nucleotide occupancy in the induction of a conformational change in tubulin. The debate has organized around seemingly contradictory models. The allosteric model invokes nucleotide-dependent states of curvature in the free tubulin dimer, such that hydrolysis leads to pronounced bending and thus disruption of the lattice. The more recent lattice model describes a predominant role for the lattice in straightening free dimers that are curved regardless of their nucleotide state. In this model, lattice-

SUBMITTER: Bennett MJ 

PROVIDER: S-EPMC4129956 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature