  In many intracellular processes, the length distribution of microtubules is
controlled by depolymerizing motor proteins. Experiments have shown that,
following non-specific binding to the surface of a microtubule, depolymerizers
are transported to the microtubule tip(s) by diffusion or directed walk and,
then, depolymerize the microtubule from the tip(s) after accumulating there. We
develop a quantitative model to study the depolymerizing action of such a
generic motor protein, and its possible effects on the length distribution of
microtubules. We show that, when the motor protein concentration in solution
exceeds a critical value, a steady state is reached where the length
distribution is, in general, non-monotonic with a single peak. However, for
highly processive motors and large motor densities, this distribution
effectively becomes an exponential decay. Our findings suggest that such motor
proteins may be selectively used by the cell to ensure precise control of MT
lengths. The model is also used to analyze experimental observations of
motor-induced depolymerization.
