Skip to content.

TUD

search  |  internal  |  deutsch
Personal tools
TU Dresden » Faculty of Mechanical Science and Engineering » Institute for Materials Science » Chair of Materials Science and Nanotechnology



Friday, 12 March 2004
(at 10:30 in room B)
Add to your Google Calendar


Filament depolymerization by motor molecules

Gernot Klein


Max-Planck-Institut fuer Physik komplexer Systeme, Dresden
  Germany  






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),(2).

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, Vol 11, 445-457, 2003.

(2) R. Ohi, M.L. Coughlin, W.S. Lane, T. Mitchison; Dev. Cell, Vol.5, 309-321, 2003.



abstract (html)

Within the DPG Frühjahrstagung 2004 (German Physical Society, Spring Meeting 2004)

last modified: 2018.10.24 Mi
author: webadmin