Motor proteins are specialized molecules which bind to
filaments of the cytoskeleton and are able to generate
forces. An unusual protein, closely related to kinesin
motors is MCAK, which binds to microtubule ends and
depolymerizes them [1]. We study the process of MCAK
binding to microtubules and subsequent depolymerization
using stochastic models. Computer simulations of a
one-dimensional hopping model are compared to the
mean-field theory of the adopted discrete model. Our
theory can explain how molecules accumulate at
depolymerizing ends.
[1] A. W. Hunter, M. Caplow,
D. L. Coy, W. O. Hancock, S. Diez, L. Wordeman, J.
Howard, Mol. Cell. 11, 445-457 (2003); R. Ohi,
M. L. Coughlin, W. S. Lane, T. Mitchison, Dev. Cell.
5, 309-321 (2003).
