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TU Dresden » Faculty of Mechanical Science and Engineering » Institute for Materials Science » Chair of Materials Science and Nanotechnology

» presentations   » 2004.03.08-12

Filament depolymerization by motor molecules

G. A. Klein, G. Cuniberti, K. Kruse, and F. Jülicher

Deutsche Physikalische Gesellschaft, AKF Frühjahrstagung 2004
German Physical Society, Spring Meeting 2004

2004.03.08-12; Regensburg, 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]. 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).

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