title: Opposite-end behaviour of dynamic microtubules.
abstract: Microtubules are dynamic polar structures with different kinetic properties at the two ends. The inherent asymmetry of the microtubule lattice determines that the relationship between the addition reaction of tubulin-GTP and the associated hydrolysis of a tubulin-GTP on the polymer is different at the two ends of the microtubule. We present a unified treatment for both ends of the microtubule, using the principles of the Lateral Cap formulation for microtubule dynamic instability. This shows that the two ends can exhibit significantly different dynamic properties in terms of amplitudes and lifetimes of growth and shrinking, depending on the relative importance of longitudinal and lateral contacts in the coupling of tubulin-GTP hydrolysis. These predictions are readily amenable to experimental verification. This modelling suggests that fine details of the subunit-subunit interactions at the microtubule end can determine the characteristic differences in kinetic behaviour of the opposite ends of dynamic microtubules. Variation of these interactions would provide a potentially sensitive general mechanism for the control of such dynamics, both in vitro and in vivo.
authors.affiliation: Division of Physical Biochemistry, National Institute for Medical Research, Mill Hill, London, U.K.
authors.forename: S R
authors.initials: SR
authors.lastname: Martin
authors.forename: M J
authors.initials: MJ
authors.lastname: Schilstra
authors.forename: P M
authors.initials: PM
authors.lastname: Bayley
mesh_terms: D001665:Binding Sites; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008870:Microtubules / Q000378:metabolism* / Q000648:ultrastructure; D008958:Models, Molecular; D014404:Tubulin / Q000378:metabolism
chemical_list: D014404:Tubulin; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate