title: Effect of tubulin diffusion on polymerization of microtubules.
abstract: The dynamics of microtubules (MT's) growing from a nucleation center is simulated with a kinetic Monte Carlo model that includes tubulin diffusion. In the limit of fast diffusion (homogeneous tubulin concentration), MT growth is synchronous and bounded. The microtubules form an aster with a monotonously decreasing long-time distribution of lengths. Slow tubulin diffusion leads to rapid dephasing in the growth dynamics, unbounded growth of some MT's, spatial inhomogeneities, and morphological change toward a morphology with bounded short MT's located in the nucleation center and unbounded long MT's with narrowly distributed lengths. The transition from unbounded to bounded growth is driven by the competition between the reaction rate of the tubulin assembly and the tubulin's diffusion rate. While the present study reports the effect of the tubulin diffusion coefficient on the transition, the results of the simulations are qualitatively comparable to the morphological and dynamical changes of centrosome-nucleated MT's from interphase to mitosis in cellular systems where the transition is regulated by the reaction rates.
authors.affiliation: Department of Materials Science and Engineering, The University of Arizona, Tucson, Arizona 85721, USA.
authors.forename: P A
authors.initials: PA
authors.lastname: Deymier
authors.forename: Y
authors.initials: Y
authors.lastname: Yang
authors.forename: J
authors.initials: J
authors.lastname: Hoying
mesh_terms: D001665:Binding Sites; D001704:Biopolymers / Q000737:chemistry*; D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D004058:Diffusion; D019281:Dimerization; D008870:Microtubules / Q000737:chemistry*; D008954:Models, Biological; D008956:Models, Chemical; D046912:Multiprotein Complexes / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D014404:Tubulin / Q000737:chemistry*
chemical_list: D001704:Biopolymers; D046912:Multiprotein Complexes; D014404:Tubulin